메뉴 건너뛰기




Volumn 5, Issue 3, 2016, Pages

Multiple roles of the small GTPase Rab7

Author keywords

Apoptosis; Autophagy; Endocytosis; Intermediate filaments; Lipophagy; Lysosome; Membrane traffic; Mitophagy; Rab7; Vesicular transport

Indexed keywords

MAMMALIAN TARGET OF RAPAMYCIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; RAB7 PROTEIN; SNARE PROTEIN; SOMATOMEDIN C;

EID: 85117871479     PISSN: None     EISSN: 20734409     Source Type: Journal    
DOI: 10.3390/cells5030034     Document Type: Review
Times cited : (295)

References (241)
  • 1
    • 80054758176 scopus 로고    scopus 로고
    • Involvement of members of the Rab family and related small GTPases in autophagosome formation and maturation
    • Chua, C.E.; Gan, B.Q.; Tang, B.L. Involvement of members of the Rab family and related small GTPases in autophagosome formation and maturation. Cell. Mol. Life Sci. 2011, 68, 3349–3358.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 3349-3358
    • Chua, C.E.1    Gan, B.Q.2    Tang, B.L.3
  • 2
    • 80052642324 scopus 로고    scopus 로고
    • Rab GTPases as regulators of endocytosis, targets of disease and therapeutic opportunities
    • Agola, J.; Jim, P.; Ward, H.; Basuray, S.; Wandinger-Ness, A. Rab GTPases as regulators of endocytosis, targets of disease and therapeutic opportunities. Clin. Genet. 2011, 80, 305–318.
    • (2011) Clin. Genet. , vol.80 , pp. 305-318
    • Agola, J.1    Jim, P.2    Ward, H.3    Basuray, S.4    Wandinger-Ness, A.5
  • 3
    • 78751701335 scopus 로고    scopus 로고
    • Rab GTPases implicated in inherited and acquired disorders
    • Mitra, S.; Cheng, K.W.; Mills, G.B. Rab GTPases implicated in inherited and acquired disorders. Semin. Cell Dev. Biol. 2011, 22, 57–68.
    • (2011) Semin. Cell Dev. Biol. , vol.22 , pp. 57-68
    • Mitra, S.1    Cheng, K.W.2    Mills, G.B.3
  • 4
    • 79956095420 scopus 로고    scopus 로고
    • Autophagosome formation and molecular mechanism of autophagy
    • Tanida, I. Autophagosome formation and molecular mechanism of autophagy. Antioxid. Redox Signal. 2011, 14, 2201–2214.
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 2201-2214
    • Tanida, I.1
  • 5
    • 84874433733 scopus 로고    scopus 로고
    • Regulation of small GTPases by GEFs, GAPs, and GDIs
    • Cherfils, J.; Zeghouf, M. Regulation of small GTPases by GEFs, GAPs, and GDIs. Physiol. Rev. 2013, 93, 269–309.
    • (2013) Physiol. Rev. , vol.93 , pp. 269-309
    • Cherfils, J.1    Zeghouf, M.2
  • 6
    • 34249018367 scopus 로고    scopus 로고
    • GEFs and GAPs: Critical elements in the control of small G proteins
    • Bos, J.L.; Rehmann, H.; Wittinghofer, A. GEFs and GAPs: Critical elements in the control of small G proteins. Cell 2007, 129, 865–877.
    • (2007) Cell , vol.129 , pp. 865-877
    • Bos, J.L.1    Rehmann, H.2    Wittinghofer, A.3
  • 8
    • 0025974686 scopus 로고
    • Rab5 controls early endosome fusion in vitro
    • Gorvel, J.P.; Chavrier, P.; Zerial, M.; Gruenberg, J. Rab5 controls early endosome fusion in vitro. Cell 1991, 64, 915–925.
    • (1991) Cell , vol.64 , pp. 915-925
    • Gorvel, J.P.1    Chavrier, P.2    Zerial, M.3    Gruenberg, J.4
  • 9
    • 0026744303 scopus 로고
    • The small GTPase Rab5 functions as a regulatory factor in the early endocytic pathway
    • Bucci, C.; Parton, R.G.; Mather, I.H.; Stunnenberg, H.; Simons, K.; Hoflack, B.; Zerial, M. The small GTPase Rab5 functions as a regulatory factor in the early endocytic pathway. Cell 1992, 70, 715–728.
    • (1992) Cell , vol.70 , pp. 715-728
    • Bucci, C.1    Parton, R.G.2    Mather, I.H.3    Stunnenberg, H.4    Simons, K.5    Hoflack, B.6    Zerial, M.7
  • 10
    • 0033580299 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 is a core component of endosome docking
    • Christoforidis, S.; McBride, H.M.; Burgoyne, R.D.; Zerial, M. The Rab5 effector EEA1 is a core component of endosome docking. Nature 1999, 397, 621–625.
    • (1999) Nature , vol.397 , pp. 621-625
    • Christoforidis, S.1    McBride, H.M.2    Burgoyne, R.D.3    Zerial, M.4
  • 12
    • 32644434386 scopus 로고    scopus 로고
    • Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early endosome motility and is up-regulated in Huntington’s disease
    • Pal, A.; Severin, F.; Lommer, B.; Shevchenko, A.; Zerial, M. Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early endosome motility and is up-regulated in Huntington’s disease. J. Cell Biol. 2006, 172, 605–618.
    • (2006) J. Cell Biol. , vol.172 , pp. 605-618
    • Pal, A.1    Severin, F.2    Lommer, B.3    Shevchenko, A.4    Zerial, M.5
  • 14
    • 0026446550 scopus 로고
    • Reversible phosphorylation—Dephosphorylation determines the localization of Rab4 during the cell cycle
    • Van der Sluijs, P.; Hull, M.; Huber, L.A.; Male, P.; Goud, B.; Mellman, I. Reversible phosphorylation—Dephosphorylation determines the localization of Rab4 during the cell cycle. EMBO J. 1992, 11, 4379–4389.
    • (1992) EMBO J. , vol.11 , pp. 4379-4389
    • Van Der Sluijs, P.1    Hull, M.2    Huber, L.A.3    Male, P.4    Goud, B.5    Mellman, I.6
  • 15
    • 0033525930 scopus 로고    scopus 로고
    • The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions
    • Sheff, D.R.; Daro, E.A.; Hull, M.; Mellman, I. The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions. J. Cell Biol. 1999, 145, 123–139.
    • (1999) J. Cell Biol. , vol.145 , pp. 123-139
    • Sheff, D.R.1    Daro, E.A.2    Hull, M.3    Mellman, I.4
  • 16
    • 74749099537 scopus 로고    scopus 로고
    • The early endosome: A busy sorting station for proteins at the crossroads
    • Jovic, M.; Sharma, M.; Rahajeng, J.; Caplan, S. The early endosome: A busy sorting station for proteins at the crossroads. Histol. Histopathol. 2010, 25, 99–112.
    • (2010) Histol. Histopathol. , vol.25 , pp. 99-112
    • Jovic, M.1    Sharma, M.2    Rahajeng, J.3    Caplan, S.4
  • 17
    • 0035798385 scopus 로고    scopus 로고
    • Evolution of the Rab family of small GTP-binding proteins
    • Pereira-Leal, J.B.; Seabra, M.C. Evolution of the Rab family of small GTP-binding proteins. J. Mol. Biol. 2001, 313, 889–901.
    • (2001) J. Mol. Biol. , vol.313 , pp. 889-901
    • Pereira-Leal, J.B.1    Seabra, M.C.2
  • 18
    • 0034714098 scopus 로고    scopus 로고
    • The mammalian Rab family of small GTPases: Definition of family and subfamily sequence motifs suggests a mechanism for functional specificity in the Ras superfamily
    • Pereira-Leal, J.B.; Seabra, M.C. The mammalian Rab family of small GTPases: Definition of family and subfamily sequence motifs suggests a mechanism for functional specificity in the Ras superfamily. J. Mol. Biol. 2000, 301, 1077–1087.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1077-1087
    • Pereira-Leal, J.B.1    Seabra, M.C.2
  • 21
    • 84865196725 scopus 로고    scopus 로고
    • Dynamics of Rab7b-dependent transport of sorting receptors
    • Progida, C.; Nielsen, M.S.; Koster, G.; Bucci, C.; Bakke, O. Dynamics of Rab7b-dependent transport of sorting receptors. Traffic 2012, 13, 1273–1285.
    • (2012) Traffic , vol.13 , pp. 1273-1285
    • Progida, C.1    Nielsen, M.S.2    Koster, G.3    Bucci, C.4    Bakke, O.5
  • 22
    • 84893742386 scopus 로고    scopus 로고
    • Rab7 is functionally required for selective cargo sorting at the early endosome
    • Girard, E.; Chmiest, D.; Fournier, N.; Johannes, L.; Paul, J.L.; Vedie, B.; Lamaze, C. Rab7 is functionally required for selective cargo sorting at the early endosome. Traffic 2014, 15, 309–326.
    • (2014) Traffic , vol.15 , pp. 309-326
    • Girard, E.1    Chmiest, D.2    Fournier, N.3    Johannes, L.4    Paul, J.L.5    Vedie, B.6    Lamaze, C.7
  • 24
    • 84891747382 scopus 로고    scopus 로고
    • The machinery of macroautophagy
    • Feng, Y.; He, D.; Yao, Z.; Klionsky, D.J. The machinery of macroautophagy. Cell Res. 2014, 24, 24–41.
    • (2014) Cell Res , vol.24 , pp. 24-41
    • Feng, Y.1    He, D.2    Yao, Z.3    Klionsky, D.J.4
  • 25
    • 0141920730 scopus 로고    scopus 로고
    • Rab7 prevents growth factor-independent survival by inhibiting cell-autonomous nutrient transporter expression
    • Edinger, A.L.; Cinalli, R.M.; Thompson, C.B. Rab7 prevents growth factor-independent survival by inhibiting cell-autonomous nutrient transporter expression. Dev. Cell 2003, 5, 571–582.
    • (2003) Dev. Cell , vol.5 , pp. 571-582
    • Edinger, A.L.1    Cinalli, R.M.2    Thompson, C.B.3
  • 26
    • 28044444522 scopus 로고    scopus 로고
    • The small GTPase Rab7 controls the endosomal trafficking and neuritogenic signaling of the nerve growth factor receptor Trka
    • Saxena, S.; Bucci, C.; Weis, J.; Kruttgen, A. The small GTPase Rab7 controls the endosomal trafficking and neuritogenic signaling of the nerve growth factor receptor Trka. J. Neurosci. 2005, 25, 10930–10940.
    • (2005) J. Neurosci , vol.25 , pp. 10930-10940
    • Saxena, S.1    Bucci, C.2    Weis, J.3    Kruttgen, A.4
  • 28
    • 0042691817 scopus 로고    scopus 로고
    • Phagosomes fuse with late endosomes and/or lysosomes by extension of membrane protrusions along microtubules: Role of rab7 and rilp
    • Harrison, R.; Bucci, C.; Vieira, O.; Schroer, T.; Grinstein, S. Phagosomes fuse with late endosomes and/or lysosomes by extension of membrane protrusions along microtubules: Role of rab7 and rilp. Mol. Cell Biol. 2003, 23, 6494–6506.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 6494-6506
    • Harrison, R.1    Bucci, C.2    Vieira, O.3    Schroer, T.4    Grinstein, S.5
  • 29
    • 84898652320 scopus 로고    scopus 로고
    • Mitochondrial Rab GAPs govern autophagosome biogenesis during mitophagy
    • Yamano, K.; Fogel, A.I.; Wang, C.; van der Bliek, A.M.; Youle, R.J. Mitochondrial Rab GAPs govern autophagosome biogenesis during mitophagy. Elife 2014, 3, e01612.
    • (2014) Elife , vol.3
    • Yamano, K.1    Fogel, A.I.2    Wang, C.3    Van Der Bliek, A.M.4    Youle, R.J.5
  • 31
    • 0242266901 scopus 로고    scopus 로고
    • A role for Rab7 GTPase in growth factor-regulated cell nutrition and apoptosis
    • Snider, M.D. A role for Rab7 GTPase in growth factor-regulated cell nutrition and apoptosis. Mol. Cell 2003, 12, 796–797.
    • (2003) Mol. Cell , vol.12 , pp. 796-797
    • Snider, M.D.1
  • 34
    • 84870197354 scopus 로고    scopus 로고
    • Molecular basis of Charcot-Marie-Tooth type 2b disease
    • Bucci, C.; De Luca, M. Molecular basis of Charcot-Marie-Tooth type 2b disease. Biochem. Soc. Trans. 2012, 40, 1368–1372.
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 1368-1372
    • Bucci, C.1    De Luca, M.2
  • 35
    • 80052233389 scopus 로고    scopus 로고
    • Endosome maturation
    • Huotari, J.; Helenius, A. Endosome maturation. EMBO J. 2011, 30, 3481–3500.
    • (2011) EMBO J , vol.30 , pp. 3481-3500
    • Huotari, J.1    Helenius, A.2
  • 36
    • 33644764063 scopus 로고    scopus 로고
    • Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes
    • Lakadamyali, M.; Rust, M.J.; Zhuang, X. Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes. Cell 2006, 124, 997–1009.
    • (2006) Cell , vol.124 , pp. 997-1009
    • Lakadamyali, M.1    Rust, M.J.2    Zhuang, X.3
  • 39
    • 79955915763 scopus 로고    scopus 로고
    • Fission of tubular endosomes triggers endosomal acidification and movement
    • Mesaki, K.; Tanabe, K.; Obayashi, M.; Oe, N.; Takei, K. Fission of tubular endosomes triggers endosomal acidification and movement. PLoS ONE 2011, 10, e19764.
    • (2011) Plos ONE , vol.10
    • Mesaki, K.1    Tanabe, K.2    Obayashi, M.3    Oe, N.4    Takei, K.5
  • 40
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • Rink, J.; Ghigo, E.; Kalaidzidis, Y.; Zerial, M. Rab conversion as a mechanism of progression from early to late endosomes. Cell 2005, 122, 735–749.
    • (2005) Cell , vol.122 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 41
    • 22744447453 scopus 로고    scopus 로고
    • Rab7 associates with early endosomes to mediate sorting and transport of Semliki orest virus to late endosomes
    • Vonderheit, A.; Helenius, A. Rab7 associates with early endosomes to mediate sorting and transport of Semliki orest virus to late endosomes. PLoS Biol. 2005, 3, e233.
    • (2005) Plos Biol. , vol.3
    • Vonderheit, A.1    Helenius, A.2
  • 42
    • 77951918362 scopus 로고    scopus 로고
    • Identification of the switch in early-to-late endosome transition
    • Poteryaev, D.; Datta, S.; Ackema, K.; Zerial, M.; Spang, A. Identification of the switch in early-to-late endosome transition. Cell 2010, 141, 497–508.
    • (2010) Cell , vol.141 , pp. 497-508
    • Poteryaev, D.1    Datta, S.2    Ackema, K.3    Zerial, M.4    Spang, A.5
  • 43
    • 17344377424 scopus 로고    scopus 로고
    • A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function
    • Horiuchi, H.; Lippé, R.; McBride, H.M.; Rubino, M.; Woodman, P.; Stenmark, H.; Rybin, V.; Wilm, M.; Ashman, K.; Mann, M., et al. A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function. Cell 1997, 90, 1149–1159.
    • (1997) Cell , vol.90 , pp. 1149-1159
    • Horiuchi, H.1    Lippé, R.2    McBride, H.M.3    Rubino, M.4    Woodman, P.5    Stenmark, H.6    Rybin, V.7    Wilm, M.8    Ashman, K.9    Mann, M.10
  • 45
    • 0035171352 scopus 로고    scopus 로고
    • Functional synergy between Rab5 effector Rabaptin-5 and exchange factor Rabex-5 when physically associated in a complex
    • Lippe, R.; Miaczynska, M.; Rybin, V.; Runge, A.; Zerial, M. Functional synergy between Rab5 effector Rabaptin-5 and exchange factor Rabex-5 when physically associated in a complex. Mol. Biol. Cell 2001, 12, 2219–2228.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2219-2228
    • Lippe, R.1    Miaczynska, M.2    Rybin, V.3    Runge, A.4    Zerial, M.5
  • 47
    • 77950460749 scopus 로고    scopus 로고
    • Identification of two evolutionarily conserved genes regulating processing of engulfed apoptotic cells
    • Kinchen, J.M.; Ravichandran, K.S. Identification of two evolutionarily conserved genes regulating processing of engulfed apoptotic cells. Nature 2010, 464, 778–782.
    • (2010) Nature , vol.464 , pp. 778-782
    • Kinchen, J.M.1    Ravichandran, K.S.2
  • 53
    • 84941356670 scopus 로고    scopus 로고
    • A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly
    • Baker, R.W.; Jeffrey, P.D.; Zick, M.; Phillips, B.P.; Wickner, W.T.; Hughson, F.M. A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly. Science 2015, 349, 1111–1114.
    • (2015) Science , vol.349 , pp. 1111-1114
    • Baker, R.W.1    Jeffrey, P.D.2    Zick, M.3    Phillips, B.P.4    Wickner, W.T.5    Hughson, F.M.6
  • 54
    • 33646128965 scopus 로고    scopus 로고
    • Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p
    • Stroupe, C.; Collins, K.M.; Fratti, R.A.; Wickner, W. Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p. EMBO J. 2006, 25, 1579–1589.
    • (2006) EMBO J , vol.25 , pp. 1579-1589
    • Stroupe, C.1    Collins, K.M.2    Fratti, R.A.3    Wickner, W.4
  • 55
    • 84923830331 scopus 로고    scopus 로고
    • The habc domain of the SNARE Vam3 interacts with the HOPS tethering complex to facilitate vacuole fusion
    • Lürick, A.; Kuhlee, A.; Bröcker, C.; Kümmel, D.; Raunser, S.; Ungermann, C. The habc domain of the SNARE Vam3 interacts with the HOPS tethering complex to facilitate vacuole fusion. J. Biol. Chem. 2015, 290, 5405–5413.
    • (2015) J. Biol. Chem , vol.290 , pp. 5405-5413
    • Lürick, A.1    Kuhlee, A.2    Bröcker, C.3    Kümmel, D.4    Raunser, S.5    Ungermann, C.6
  • 56
    • 0034662876 scopus 로고    scopus 로고
    • Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion
    • Seals, D.F.; Eitzen, G.; Margolis, N.; Wickner, W.T.; Price, A. A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion. Proc. Natl. Acad. Sci. USA 2000, 97, 9402–9407.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9402-9407
    • Seals, D.F.1    Eitzen, G.2    Margolis, N.3    Wickner, W.T.4    Price, A.A.5
  • 58
    • 84945298509 scopus 로고    scopus 로고
    • Three steps forward, two steps back: Mechanistic insights into the assembly and disassembly of the SNARE complex
    • Bombardier, J.P.; Munson, M. Three steps forward, two steps back: Mechanistic insights into the assembly and disassembly of the SNARE complex. Curr. Opin. Chem. Biol. 2015, 29, 66–71.
    • (2015) Curr. Opin. Chem. Biol , vol.29 , pp. 66-71
    • Bombardier, J.P.1    Munson, M.2
  • 59
    • 84950341301 scopus 로고    scopus 로고
    • Characterization of the mammalian CORVET and HOPS complexes and their modular restructuring for endosome specificity
    • Van der Kant, R.; Jonker, C.T.; Wijdeven, R.H.; Bakker, J.; Janssen, L.; Klumperman, J.; Neefjes, J. Characterization of the mammalian CORVET and HOPS complexes and their modular restructuring for endosome specificity. J. Biol. Chem. 2015, 290, 30280–30290.
    • (2015) J. Biol. Chem , vol.290 , pp. 30280-30290
    • Van Der Kant, R.1    Jonker, C.T.2    Wijdeven, R.H.3    Bakker, J.4    Janssen, L.5    Klumperman, J.6    Neefjes, J.7
  • 61
    • 84929496869 scopus 로고    scopus 로고
    • RILP interacts with HOPS complex via Vps41 subunit to regulate endocytic trafficking
    • Lin, X.; Yang, T.; Wang, S.; Wang, Z.; Yun, Y.; Sun, L.; Zhou, Y.; Xu, X.; Akazawa, C.; Hong, W., et al. RILP interacts with HOPS complex via Vps41 subunit to regulate endocytic trafficking. Sci. Rep. 2014, 4, 7282.
    • (2014) Sci. Rep. , vol.4 , pp. 7282
    • Lin, X.1    Yang, T.2    Wang, S.3    Wang, Z.4    Yun, Y.5    Sun, L.6    Zhou, Y.7    Xu, X.8    Akazawa, C.9    Hong, W.10
  • 62
    • 84929486075 scopus 로고    scopus 로고
    • The small GTPase Arl8b regulates assembly of the mammalian HOPS complex to lysosomes
    • Khatter, D.; Raina, V.B.; Dwivedi, D.; Sindhwani, A.; Bahl, S.; Sharma, M. The small GTPase Arl8b regulates assembly of the mammalian HOPS complex to lysosomes. J. Cell Sci. 2015, 128, 1746–1761.
    • (2015) J. Cell Sci. , vol.128 , pp. 1746-1761
    • Khatter, D.1    Raina, V.B.2    Dwivedi, D.3    Sindhwani, A.4    Bahl, S.5    Sharma, M.6
  • 63
    • 0344851732 scopus 로고    scopus 로고
    • Roles of the cytoskeleton and motor proteins in endocytic sorting
    • Murray, J.W.; Wolkoff, A.W. Roles of the cytoskeleton and motor proteins in endocytic sorting. Adv. Drug Deliv. Rev. 2003, 55, 1385–1403.
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 1385-1403
    • Murray, J.W.1    Wolkoff, A.W.2
  • 64
    • 73349125122 scopus 로고    scopus 로고
    • Tug-of-war between dissimilar teams of microtubule motors regulates transport and fission of endosomes
    • Soppina, V.; Rai, A.K.; Ramaiya, A.J.; Barak, P.; Mallik, R. Tug-of-war between dissimilar teams of microtubule motors regulates transport and fission of endosomes. Proc. Natl. Acad. Sci. USA 2009, 106, 19381–19386.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 19381-19386
    • Soppina, V.1    Rai, A.K.2    Ramaiya, A.J.3    Barak, P.4    Mallik, R.5
  • 65
    • 0029869843 scopus 로고    scopus 로고
    • An endosomal _-COP is involved in the pH-dependent formation of transport vesicles destined for late endosomes
    • Aniento, F.; Gu, F.; Parton, R.G.; Gruenberg, J. An endosomal _-COP is involved in the pH-dependent formation of transport vesicles destined for late endosomes. J. Cell Biol. 1996, 133, 29–41.
    • (1996) J. Cell Biol , vol.133 , pp. 29-41
    • Aniento, F.1    Gu, F.2    Parton, R.G.3    Gruenberg, J.4
  • 67
    • 0035865135 scopus 로고    scopus 로고
    • Rab-interacting lysosomal protein (RILP): The Rab7 effector required for transport to lysosomes
    • Cantalupo, G.; Alifano, P.; Roberti, V.; Bruni, C.B.; Bucci, C. Rab-interacting lysosomal protein (RILP): The Rab7 effector required for transport to lysosomes. EMBO J. 2001, 20, 683–693.
    • (2001) EMBO J , vol.20 , pp. 683-693
    • Cantalupo, G.1    Alifano, P.2    Roberti, V.3    Bruni, C.B.4    Bucci, C.5
  • 69
    • 33847003020 scopus 로고    scopus 로고
    • Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150glued, ORP1L, and the receptor betaIII spectrin
    • Johansson, M.; Rocha, N.; Zwart, W.; Jordens, I.; Janssen, L.; Kuijl, C.; Olkkonen, V.M.; Neefjes, J. Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150glued, ORP1L, and the receptor betaIII spectrin. J. Cell Biol. 2007, 176, 459–471.
    • (2007) J. Cell Biol. , vol.176 , pp. 459-471
    • Johansson, M.1    Rocha, N.2    Zwart, W.3    Jordens, I.4    Janssen, L.5    Kuijl, C.6    Olkkonen, V.M.7    Neefjes, J.8
  • 70
    • 76149086512 scopus 로고    scopus 로고
    • FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport
    • Pankiv, S.; Alemu, E.A.; Brech, A.; Bruun, J.A.; Lamark, T.; Overvatn, A.; Bjørkøy, G.; Johansen, T. FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport. J. Cell Biol. 2010, 188, 253–269.
    • (2010) J. Cell Biol , vol.188 , pp. 253-269
    • Pankiv, S.1    Alemu, E.A.2    Brech, A.3    Bruun, J.A.4    Lamark, T.5    Overvatn, A.6    Bjørkøy, G.7    Johansen, T.8
  • 71
    • 0030298068 scopus 로고    scopus 로고
    • The biogenesis of lysosomes: Is it a kiss and run, continuous fusion and fission process?
    • Storrie, B.; Desjardins, M. The biogenesis of lysosomes: Is it a kiss and run, continuous fusion and fission process? Bioessays 1996, 18, 895–903.
    • (1996) Bioessays , vol.18 , pp. 895-903
    • Storrie, B.1    Desjardins, M.2
  • 72
    • 0029585762 scopus 로고
    • Rab 7: An important regulator of late endocytic membrane traffic
    • Feng, Y.; Press, B.; Wandinger-Ness, A. Rab 7: An important regulator of late endocytic membrane traffic. J. Cell Biol 1995, 131, 1435–1452.
    • (1995) J. Cell Biol , vol.131 , pp. 1435-1452
    • Feng, Y.1    Press, B.2    Wandinger-Ness, A.3
  • 73
    • 0032498795 scopus 로고    scopus 로고
    • Mutant Rab7 causes the accumulation of cathepsin D and cation-independent mannose 6-phosphate receptor in an early endocytic compartment
    • Press, B.; Feng, Y.; Hoflack, B.; Wandinger-Ness, A. Mutant Rab7 causes the accumulation of cathepsin D and cation-independent mannose 6-phosphate receptor in an early endocytic compartment. J. Cell Biol. 1998, 140, 1075–1089.
    • (1998) J. Cell Biol. , vol.140 , pp. 1075-1089
    • Press, B.1    Feng, Y.2    Hoflack, B.3    Wandinger-Ness, A.4
  • 74
    • 0028803110 scopus 로고
    • The Rab7 GTPase resides on a vesicular compartment connected to lysosomes
    • Meresse, S.; Gorvel, G.P.; Chavrier, P. The Rab7 GTPase resides on a vesicular compartment connected to lysosomes. J. Cell Sci. 1995, 108, 3349–3358.
    • (1995) J. Cell Sci , vol.108 , pp. 3349-3358
    • Meresse, S.1    Gorvel, G.P.2    Chavrier, P.3
  • 76
    • 33644869303 scopus 로고    scopus 로고
    • Rab7 activity affects epidermal growth factor: Epidermal growth factor receptor degradation by regulating endocytic trafficking from the late endosome
    • Ceresa, B.P.; Bahr, S.J. Rab7 activity affects epidermal growth factor: Epidermal growth factor receptor degradation by regulating endocytic trafficking from the late endosome. J. Biol. Chem. 2006, 281, 1099–1106.
    • (2006) J. Biol. Chem , vol.281 , pp. 1099-1106
    • Ceresa, B.P.1    Bahr, S.J.2
  • 77
    • 66449123730 scopus 로고    scopus 로고
    • Rab7 regulates late endocytic trafficking downstream of multivesicular body biogenesis and cargo sequestration
    • Vanlandingham, P.A.; Ceresa, B.P. Rab7 regulates late endocytic trafficking downstream of multivesicular body biogenesis and cargo sequestration. J. Biol. Chem. 2009, 284, 12110–12124.
    • (2009) J. Biol. Chem , vol.284 , pp. 12110-12124
    • Vanlandingham, P.A.1    Ceresa, B.P.2
  • 78
    • 0022555867 scopus 로고
    • Acidification of the endocytic and exocytic pathways
    • Mellman, I.; Fuchs, R.; Helenius, A. Acidification of the endocytic and exocytic pathways. Annu. Rev. Biochem. 1986, 55, 663–700.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 663-700
    • Mellman, I.1    Fuchs, R.2    Helenius, A.3
  • 79
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • Forgac, M. Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol. 2007, 8, 917–929.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 917-929
    • Forgac, M.1
  • 80
    • 84914145216 scopus 로고    scopus 로고
    • The vacuolar-type H-ATPase at a glance—More than a proton pump
    • Maxson, M.E.; Grinstein, S. The vacuolar-type H-ATPase at a glance—More than a proton pump. J. Cell Sci. 2014, 127, 4987–4993.
    • (2014) J. Cell Sci , vol.127 , pp. 4987-4993
    • Maxson, M.E.1    Grinstein, S.2
  • 81
    • 84919932988 scopus 로고    scopus 로고
    • A new V-ATPase regulatory mechanism mediated by the Rab interacting lysosomal protein (RILP)
    • De Luca, M.; Bucci, C. A new V-ATPase regulatory mechanism mediated by the Rab interacting lysosomal protein (RILP). Commun. Integr. Biol. 2014, 7, 1–4.
    • (2014) Commun. Integr. Biol. , vol.7 , pp. 1-4
    • De Luca, M.1    Bucci, C.2
  • 83
    • 84978796152 scopus 로고    scopus 로고
    • The position of lysosomes within the cell determines their luminal pH
    • Johnson, D.E.; Ostrowski, P.; Jaumouillé, V.; Grinstein, S. The position of lysosomes within the cell determines their luminal pH. J. Cell Biol. 2016, 212, 677–692.
    • (2016) J. Cell Biol , vol.212 , pp. 677-692
    • Johnson, D.E.1    Ostrowski, P.2    Jaumouillé, V.3    Grinstein, S.4
  • 84
    • 38549158099 scopus 로고    scopus 로고
    • Phagocytosis and comparative innate immunity: Learning on the fly
    • Stuart, L.M.; Ezekowitz, R.A. Phagocytosis and comparative innate immunity: Learning on the fly. Nat. Rev. Immunol. 2008, 8, 131–141.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 131-141
    • Stuart, L.M.1    Ezekowitz, R.A.2
  • 85
    • 36448961645 scopus 로고    scopus 로고
    • Engulfment of apoptotic cells: Signals for a good meal
    • Ravichandran, K.S.; Lorenz, U. Engulfment of apoptotic cells: Signals for a good meal. Nat. Rev. Immunol. 2007, 7, 964–974.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 964-974
    • Ravichandran, K.S.1    Lorenz, U.2
  • 86
    • 64749091309 scopus 로고    scopus 로고
    • Antimicrobial mechanisms of phagocytes and bacterial evasion strategies
    • Flannagan, R.S.; Cosío, G.; Grinstein, S. Antimicrobial mechanisms of phagocytes and bacterial evasion strategies. Nat. Rev. Microbiol. 2009, 7, 355–366.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 355-366
    • Flannagan, R.S.1    Cosío, G.2    Grinstein, S.3
  • 88
    • 28644446115 scopus 로고    scopus 로고
    • The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments
    • Johansson, M.; Lehto, M.; Tanhuanpaa, K.; Cover, T.L.; Olkkonen, V.M. The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments. Mol. Biol. Cell 2005, 16, 5480–5492.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5480-5492
    • Johansson, M.1    Lehto, M.2    Tanhuanpaa, K.3    Cover, T.L.4    Olkkonen, V.M.5
  • 89
    • 0030960157 scopus 로고    scopus 로고
    • Arrest of mycobacterial phagosome maturation is caused by a block in vesicle fusion between stages controlled by Rab5 and Rab7
    • Via, L.E.; Deretic, D.; Ulmer, R.J.; Hibler, N.S.; Huber, L.A.; Deretic, V. Arrest of mycobacterial phagosome maturation is caused by a block in vesicle fusion between stages controlled by Rab5 and Rab7. J. Biol. Chem. 1997, 272, 13326–13331.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13326-13331
    • Via, L.E.1    Deretic, D.2    Ulmer, R.J.3    Hibler, N.S.4    Huber, L.A.5    Deretic, V.6
  • 90
    • 84946782287 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis inhibits Rab7 recruitment to selectively modulate autophagy flux in macrophages
    • Chandra, P.; Ghanwat, S.; Matta, S.K.; Yadav, S.S.; Mehta, M.; Siddiqui, Z.; Singh, A.; Kumar, D. Mycobacterium tuberculosis inhibits Rab7 recruitment to selectively modulate autophagy flux in macrophages. Sci. Rep. 2015, 5, 16320.
    • (2015) Sci. Rep. , vol.5 , pp. 16320
    • Chandra, P.1    Ghanwat, S.2    Matta, S.K.3    Yadav, S.S.4    Mehta, M.5    Siddiqui, Z.6    Singh, A.7    Kumar, D.8
  • 91
    • 33748313351 scopus 로고    scopus 로고
    • Retrograde transport from endosomes to the Trans-Golgi Network
    • Bonifacino, J.S.; Rojas, R. Retrograde transport from endosomes to the Trans-Golgi Network. Nat. Rev. Mol. Cell Biol. 2006, 7, 568–579.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 568-579
    • Bonifacino, J.S.1    Rojas, R.2
  • 93
    • 13244275069 scopus 로고    scopus 로고
    • Recycle your receptors with retromer
    • Seaman, M.N. Recycle your receptors with retromer. Trends Cell Biol. 2005, 15, 68–75.
    • (2005) Trends Cell Biol , vol.15 , pp. 68-75
    • Seaman, M.N.1
  • 94
    • 84255208762 scopus 로고    scopus 로고
    • Sorting nexins provide diversity for retromer-dependent trafficking events
    • Cullen, P.J.; Korswagen, H.C. Sorting nexins provide diversity for retromer-dependent trafficking events. Nat. Cell Biol. 2012, 14, 29–37.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 29-37
    • Cullen, P.J.1    Korswagen, H.C.2
  • 96
    • 0033634771 scopus 로고    scopus 로고
    • Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: Assembly into multimeric complexes
    • Haft, C.R.; de la Luz Sierra, M.; Bafford, R.; Lesniak, M.A.; Barr, V.A.; Taylor, S.I. Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: Assembly into multimeric complexes. Mol. Biol. Cell 2000, 11, 4105–4116.
    • (2000) "');"> , vol.11 , pp. 4105-4116
    • Haft, C.R.1    De La Luz Sierra, M.2    Bafford, R.3    Lesniak, M.A.4    Barr, V.A.5    Taylor, S.I.6
  • 97
    • 22144490854 scopus 로고    scopus 로고
    • Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly
    • Collins, B.M.; Skinner, C.F.; Watson, P.J.; Seaman, M.N.; Owen, D.J. Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly. Nat. Struct. Mol. Biol. 2005, 12, 594–602.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 594-602
    • Collins, B.M.1    Skinner, C.F.2    Watson, P.J.3    Seaman, M.N.4    Owen, D.J.5
  • 98
    • 33846587097 scopus 로고    scopus 로고
    • Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors
    • Rojas, R.; Kametaka, S.; Haft, C.R.; Bonifacino, J.S. Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors. Mol. Cell Biol. 2007, 27, 1112–1124.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 1112-1124
    • Rojas, R.1    Kametaka, S.2    Haft, C.R.3    Bonifacino, J.S.4
  • 99
    • 0026637316 scopus 로고
    • Structure and function of the mannose 6-phosphate/insulin-like growth factor II receptors
    • Kornfeld, S. Structure and function of the mannose 6-phosphate/insulin-like growth factor II receptors. Annu. Rev. Biochem. 1992, 61, 307–330.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 307-330
    • Kornfeld, S.1
  • 100
    • 2442530398 scopus 로고    scopus 로고
    • Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor
    • Arighi, C.N.; Hartnell, L.M.; Aguilar, R.C.; Haft, C.R.; Bonifacino, J.S. Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor. J. Cell Biol. 2004, 165, 123–133.
    • (2004) J. Cell Biol , vol.165 , pp. 123-133
    • Arighi, C.N.1    Hartnell, L.M.2    Aguilar, R.C.3    Haft, C.R.4    Bonifacino, J.S.5
  • 101
    • 6944255481 scopus 로고    scopus 로고
    • Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high-curvature membranes and 3-phosphoinositides
    • Carlton, J.; Bujny, M.; Peter, B.J.; Oorschot, V.M.; Rutherford, A.; Mellor, H.; Klumperman, J.; McMahon, H.T.; Cullen, P.J. Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high-curvature membranes and 3-phosphoinositides. Curr. Biol. 2004, 14, 1791–1800.
    • (2004) Curr. Biol. , vol.14 , pp. 1791-1800
    • Carlton, J.1    Bujny, M.2    Peter, B.J.3    Oorschot, V.M.4    Rutherford, A.5    Mellor, H.6    Klumperman, J.7    McMahon, H.T.8    Cullen, P.J.9
  • 102
    • 2442509574 scopus 로고    scopus 로고
    • Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer
    • Seaman, M.N. Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer. J. Cell Biol. 2004, 165, 111–122.
    • (2004) J. Cell Biol. , vol.165 , pp. 111-122
    • Seaman, M.N.1
  • 105
    • 69649083104 scopus 로고    scopus 로고
    • Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5
    • Seaman, M.N.J.; Harbour, M.E.; Tattersall, D.; Read, E.; Bright, N. Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5. J. Cell Sci. 2009, 122, 2371–2382.
    • (2009) "');"> , vol.122 , pp. 2371-2382
    • Seaman, M.N.J.1    Harbour, M.E.2    Tattersall, D.3    Read, E.4    Bright, N.5
  • 106
    • 84863535520 scopus 로고    scopus 로고
    • Rab GTPase regulation of retromer-mediated cargo export during endosome maturation
    • Liu, T.-T.; Gomez, T.S.; Sackey, B.K.; Billadeau, D.D.; Burd, C.G. Rab GTPase regulation of retromer-mediated cargo export during endosome maturation. Mol. Biol. Cell 2012, 23, 2505–2515.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 2505-2515
    • Liu, T.-T.1    Gomez, T.S.2    Sackey, B.K.3    Billadeau, D.D.4    Burd, C.G.5
  • 108
    • 0030897485 scopus 로고    scopus 로고
    • Emr, S.D. Endosome to golgi retrieval of the vacuolar protein sorting receptor, Vps10p, requires the function of the Vps29, Vps30, and Vps35 gene products
    • Seaman, M.N.; Marcusson, E.G.; Cereghino, J.L.; Emr, S.D. Endosome to golgi retrieval of the vacuolar protein sorting receptor, Vps10p, requires the function of the Vps29, Vps30, and Vps35 gene products. J. Cell Biol. 1997, 137, 79–92.
    • (1997) J. Cell Biol , vol.137 , pp. 79-92
    • Seaman, M.N.1    Marcusson, E.G.2    Cereghino, J.L.3
  • 109
    • 0029905298 scopus 로고    scopus 로고
    • Vps10p cycles between the late-golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases
    • Cooper, A.A.; Stevens, T.H. Vps10p cycles between the late-golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases. J. Cell Biol. 1996, 133, 529–541.
    • (1996) J. Cell Biol , vol.133 , pp. 529-541
    • Cooper, A.A.1    Stevens, T.H.2
  • 110
    • 84924662957 scopus 로고    scopus 로고
    • Retromer and the dynamin Vps1 cooperate in the retrieval of transmembrane proteins from vacuoles
    • Arlt, H.; Reggiori, F.; Ungermann, C. Retromer and the dynamin Vps1 cooperate in the retrieval of transmembrane proteins from vacuoles. J. Cell Sci. 2015, 128, 645–655.
    • (2015) J. Cell Sci. , vol.128 , pp. 645-655
    • Arlt, H.1    Reggiori, F.2    Ungermann, C.3
  • 111
    • 84959378767 scopus 로고    scopus 로고
    • Parkin modulates endosomal organization and function of the endo-lysosomal pathway
    • Song, P.; Trajkovic, K.; Tsunemi, T.; Krainc, D. Parkin modulates endosomal organization and function of the endo-lysosomal pathway. J. Neurosci. 2016, 36, 2425–2437.
    • (2016) J. Neurosci. , vol.36 , pp. 2425-2437
    • Song, P.1    Trajkovic, K.2    Tsunemi, T.3    Krainc, D.4
  • 112
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • Kroemer, G.; Mariño, G.; Levine, B. Autophagy and the integrated stress response. Mol. Cell 2010, 40, 280–293.
    • (2010) Mol. Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Mariño, G.2    Levine, B.3
  • 113
    • 84901826020 scopus 로고    scopus 로고
    • Mitochondrial homeostasis: The interplay between mitophagy and mitochondrial biogenesis
    • Palikaras, K.; Tavernarakis, N. Mitochondrial homeostasis: The interplay between mitophagy and mitochondrial biogenesis. Exp. Gerontol. 2014, 56, 182–188.
    • (2014) Exp. Gerontol. , vol.56 , pp. 182-188
    • Palikaras, K.1    Tavernarakis, N.2
  • 114
    • 84864313580 scopus 로고    scopus 로고
    • Autophagy in the brains of young patients with poorly controlled T1DM and fatal diabetic ketoacidosis
    • Hoffman, W.H.; Shacka, J.J.; Andjelkovic, A.V. Autophagy in the brains of young patients with poorly controlled T1DM and fatal diabetic ketoacidosis. Exp. Mol. Pathol. 2012, 93, 273–280.
    • (2012) Exp. Mol. Pathol. , vol.93 , pp. 273-280
    • Hoffman, W.H.1    Shacka, J.J.2    Andjelkovic, A.V.3
  • 119
    • 79952166584 scopus 로고    scopus 로고
    • Starvation induced cell death in autophagy-defective yeast mutants is caused by mitochondria dysfunction
    • Suzuki, S.W.; Onodera, J.; Ohsumi, Y. Starvation induced cell death in autophagy-defective yeast mutants is caused by mitochondria dysfunction. PLoS ONE 2011, 6, e17412.
    • (2011) Plos ONE , vol.6
    • Suzuki, S.W.1    Onodera, J.2    Ohsumi, Y.3
  • 122
    • 84879047011 scopus 로고    scopus 로고
    • Cellular metabolic and autophagic pathways: Traffic control by redox signaling
    • Dodson, M.; Darley-Usmar, V.; Zhang, J. Cellular metabolic and autophagic pathways: Traffic control by redox signaling. Free Radic. Biol. Med. 2013, 63, 207–221.
    • (2013) Free Radic. Biol. Med. , vol.63 , pp. 207-221
    • Dodson, M.1    Darley-Usmar, V.2    Zhang, J.3
  • 123
    • 84055178474 scopus 로고    scopus 로고
    • Regulation and function of ribosomal protein s6 kinase (S6K) within mtor signalling networks
    • Magnuson, B.; Ekim, B.; Fingar, D.C. Regulation and function of ribosomal protein s6 kinase (S6K) within mtor signalling networks. Biochem. J. 2012, 441, 1–21.
    • (2012) Biochem. J. , vol.441 , pp. 1-21
    • Magnuson, B.1    Ekim, B.2    Fingar, D.C.3
  • 124
    • 77950501014 scopus 로고    scopus 로고
    • Kim, D.H. mTOR regulation of autophagy
    • Jung, C.H.; Ro, S.H.; Cao, J.; Otto, N.M.; Kim, D.H. mTOR regulation of autophagy. FEBS Lett. 2010, 584, 1287–1295.
    • (2010) FEBS Lett , vol.584 , pp. 1287-1295
    • Jung, C.H.1    Ro, S.H.2    Cao, J.3    Otto, N.M.4
  • 125
    • 79952628267 scopus 로고    scopus 로고
    • The beclin 1 network regulates autophagy and apoptosis
    • Kang, R.; Zeh, H.J.; Lotze, M.T.; Tang, D. The beclin 1 network regulates autophagy and apoptosis. Cell Death Differ. 2011, 18, 571–580.
    • (2011) Cell Death Differ , vol.18 , pp. 571-580
    • Kang, R.1    Zeh, H.J.2    Lotze, M.T.3    Tang, D.4
  • 126
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He, C.; Klionsky, D.J. Regulation mechanisms and signaling pathways of autophagy. Annu. Rev. Genet. 2009, 43, 67–93.
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 127
    • 48949098967 scopus 로고    scopus 로고
    • New insights into the mechanisms of macroautophagy in mammalian cells
    • Eskelinen, E.L. New insights into the mechanisms of macroautophagy in mammalian cells. Int. Rev. Cell Mol. Biol. 2008, 266, 207–247.
    • (2008) Int. Rev. Cell Mol. Biol. , vol.266 , pp. 207-247
    • Eskelinen, E.L.1
  • 128
    • 0032498539 scopus 로고    scopus 로고
    • Fusion of lysosomes with late endosomes produces a hybrid organelle of intermediate density and is nsf dependent
    • Mullock, B.M.; Bright, N.A.; Faeron, C.W.; Gray, S.R.; Luzio, J.P. Fusion of lysosomes with late endosomes produces a hybrid organelle of intermediate density and is nsf dependent. J. Cell Biol. 1998, 140, 591–601.
    • (1998) J. Cell Biol. , vol.140 , pp. 591-601
    • Mullock, B.M.1    Bright, N.A.2    Faeron, C.W.3    Gray, S.R.4    Luzio, J.P.5
  • 130
    • 0028222874 scopus 로고
    • Autophagy and related mechanisms of lysosomal-mediated protein degradation
    • Dunn, W.A. Autophagy and related mechanisms of lysosomal-mediated protein degradation. Trends Cell Biol. 1994, 4, 139–143.
    • (1994) Trends Cell Biol , vol.4 , pp. 139-143
    • Dunn, W.A.1
  • 131
    • 84930375084 scopus 로고    scopus 로고
    • Recruitment of Vps33a to hops by Vps16 is required for lysosome fusion with endosomes and autophagosomes
    • Wartosch, L.; Günesdogan, U.; Graham, S.C.; Luzio, J.P. Recruitment of Vps33a to hops by Vps16 is required for lysosome fusion with endosomes and autophagosomes. Traffic 2015, 16, 727–742.
    • (2015) Traffic , vol.16 , pp. 727-742
    • Wartosch, L.1    Günesdogan, U.2    Graham, S.C.3    Luzio, J.P.4
  • 133
    • 77949448601 scopus 로고    scopus 로고
    • Combinational soluble n-ethylmaleimide-sensitive factor attachment protein receptor proteins Vamp8 and vti1b mediate fusion of antimicrobial and canonical autophagosomes with lysosomes
    • Furuta, N.; Fujita, N.; Noda, T.; Yoshimori, T.; Amano, A. Combinational soluble n-ethylmaleimide-sensitive factor attachment protein receptor proteins Vamp8 and vti1b mediate fusion of antimicrobial and canonical autophagosomes with lysosomes. Mol. Biol. Cell 2010, 21, 1001–1010.
    • (2010) "');"> , vol.21 , pp. 1001-1010
    • Furuta, N.1    Fujita, N.2    Noda, T.3    Yoshimori, T.4    Amano, A.5
  • 134
    • 84870880174 scopus 로고    scopus 로고
    • The hairpin-type tail-anchored SANRE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes
    • Itakura, E.; Kishi-Itakura, C.; Mizushima, N. The hairpin-type tail-anchored SANRE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes. Cell 2012, 151, 1256–1269.
    • (2012) Cell , vol.151 , pp. 1256-1269
    • Itakura, E.1    Kishi-Itakura, C.2    Mizushima, N.3
  • 135
    • 79451475816 scopus 로고    scopus 로고
    • Perturbation of cullin deneddylation via conditional CSN8 ablation impairs the ubiquitin-proteasome system and causes cardiomyocyte necrosis and dilated cardiomyopathy in mice
    • Su, H.; Li, J.; Menon, S.; Liu, J.; Kumarapeli, A.R.; Wei, N.; Wang, X. Perturbation of cullin deneddylation via conditional CSN8 ablation impairs the ubiquitin-proteasome system and causes cardiomyocyte necrosis and dilated cardiomyopathy in mice. Circ. Res. 2011, 108, 40–50.
    • (2011) Circ. Res. , vol.108 , pp. 40-50
    • Su, H.1    Li, J.2    Menon, S.3    Liu, J.4    Kumarapeli, A.R.5    Wei, N.6    Wang, X.7
  • 136
    • 56449094567 scopus 로고    scopus 로고
    • The COP9 signalosome: More than a protease
    • Wei, N.; Serino, G.; Deng, X.W. The COP9 signalosome: More than a protease. Trends Biochem. Sci. 2008, 33, 592–600.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 592-600
    • Wei, N.1    Serino, G.2    Deng, X.W.3
  • 137
    • 84876408458 scopus 로고    scopus 로고
    • Activation of lysosomal function in the course of autophagy via mTORC1 suppression and autophagosome-lysosome fusion
    • Zhou, J.; Tan, S.H.; Nicolas, V.; Bauvy, C.; Yang, N.D.; Zhang, J.; Xue, Y.; Codogno, P.; Shen, H.M. Activation of lysosomal function in the course of autophagy via mTORC1 suppression and autophagosome-lysosome fusion. Cell Res. 2013, 23, 508–523.
    • (2013) Cell Res. , vol.23 , pp. 508-523
    • Zhou, J.1    Tan, S.H.2    Nicolas, V.3    Bauvy, C.4    Yang, N.D.5    Zhang, J.6    Xue, Y.7    Codogno, P.8    Shen, H.M.9
  • 139
    • 3242877218 scopus 로고    scopus 로고
    • Rab7 is required for the normal progression of the autophagic pathway in mammalian cells
    • Gutierrez, M.; Munafó, D.; Berón, W.; Colombo, M. Rab7 is required for the normal progression of the autophagic pathway in mammalian cells. J. Cell Sci. 2004, 117, 2687–2697.
    • (2004) J. Cell Sci , vol.117 , pp. 2687-2697
    • Gutierrez, M.1    Munafó, D.2    Berón, W.3    Colombo, M.4
  • 140
    • 78650419576 scopus 로고    scopus 로고
    • Rab7: Role of its protein interaction cascades in endo-lysosomal traffic
    • Wang, T.; Ming, Z.; Xiaochun, W.; Hong, W. Rab7: Role of its protein interaction cascades in endo-lysosomal traffic. Cell. Signal. 2011, 23, 516–521.
    • (2011) Cell. Signal. , vol.23 , pp. 516-521
    • Wang, T.1    Ming, Z.2    Xiaochun, W.3    Hong, W.4
  • 141
    • 67749111834 scopus 로고    scopus 로고
    • Insulin-like growth factor-I prevents the accumulation of autophagic vesicles and cell death in purkinje neurons by increasing the rate of autophagosome-to-lysosome fusion and degradation
    • Bains, M.; Florez-McClure, M.L.; Heidenreich, K.A. Insulin-like growth factor-I prevents the accumulation of autophagic vesicles and cell death in purkinje neurons by increasing the rate of autophagosome-to-lysosome fusion and degradation. J. Biol. Chem. 2009, 284, 20398–20407.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20398-20407
    • Bains, M.1    Florez-McClure, M.L.2    Heidenreich, K.A.3
  • 142
    • 78650687327 scopus 로고    scopus 로고
    • IGF-I stimulates Rab7-RILP interaction during neuronal autophagy
    • Bains, M.; Zaegel, V.; Mize-Berge, J.; Heidenreich, K.A. IGF-I stimulates Rab7-RILP interaction during neuronal autophagy. Neurosci. Lett. 2011, 488, 112–117.
    • (2011) Neurosci. Lett. , vol.488 , pp. 112-117
    • Bains, M.1    Zaegel, V.2    Mize-Berge, J.3    Heidenreich, K.A.4
  • 143
    • 84857858536 scopus 로고    scopus 로고
    • Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons
    • Maday, S.; Wallace, K.E.; Holzbaur, E.L. Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons. J. Cell Biol. 2012, 196, 407–417.
    • (2012) J. Cell Biol. , vol.196 , pp. 407-417
    • Maday, S.1    Wallace, K.E.2    Holzbaur, E.L.3
  • 144
    • 84962222721 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase 2 activation in aged heart improves the autophagy by reducing the carbonyl modification on Sirt1
    • Wu, B.; Yu, L.; Wang, Y.; Wang, H.; Li, C.; Yin, Y.; Yang, J.; Wang, Z.; Zheng, Q.; Ma, H. Aldehyde dehydrogenase 2 activation in aged heart improves the autophagy by reducing the carbonyl modification on Sirt1. Oncotarget 2016, 7, 2175–2188.
    • (2016) Oncotarget , vol.7 , pp. 2175-2188
    • Wu, B.1    Yu, L.2    Wang, Y.3    Wang, H.4    Li, C.5    Yin, Y.6    Yang, J.7    Wang, Z.8    Zheng, Q.9    Ma, H.10
  • 145
    • 77956565655 scopus 로고    scopus 로고
    • Mitochondrial aldehyde dehydrogenase and cardiac diseases
    • Chen, C.H.; Sun, L.; Mochly-Rosen, D. Mitochondrial aldehyde dehydrogenase and cardiac diseases. Cardiovasc. Res. 2010, 88, 51–57.
    • (2010) Cardiovasc. Res. , vol.88 , pp. 51-57
    • Chen, C.H.1    Sun, L.2    Mochly-Rosen, D.3
  • 146
    • 84891551821 scopus 로고    scopus 로고
    • Targeting aldehyde dehydrogenase 2: New therapeutic opportunities
    • Chen, C.H.; Ferreira, J.C.; Gross, E.R.; Mochly-Rosen, D. Targeting aldehyde dehydrogenase 2: New therapeutic opportunities. Physiol. Rev. 2014, 94, 1–34.
    • (2014) Physiol. Rev. , vol.94 , pp. 1-34
    • Chen, C.H.1    Ferreira, J.C.2    Gross, E.R.3    Mochly-Rosen, D.4
  • 150
    • 0034874791 scopus 로고    scopus 로고
    • AAA proteases of mitochondria: Quality control of membrane proteins and regulatory functions during mitochondrial biogenesis
    • Langer, T.; Kaser, M.; Klanner, C.; Leonhard, K. AAA proteases of mitochondria: Quality control of membrane proteins and regulatory functions during mitochondrial biogenesis. Biochem. Soc. Trans. 2001, 29, 431–436.
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 431-436
    • Langer, T.1    Kaser, M.2    Klanner, C.3    Leonhard, K.4
  • 152
    • 84959516439 scopus 로고    scopus 로고
    • Metabolic regulation of mitochondrial dynamics
    • Mishra, P.; Chan, D.C. Metabolic regulation of mitochondrial dynamics. J. Cell Biol. 2016, 212, 379–387.
    • (2016) J. Cell Biol , vol.212 , pp. 379-387
    • Mishra, P.1    Chan, D.C.2
  • 153
    • 79954590130 scopus 로고    scopus 로고
    • Mitochondria autophagy in yeast. CORD Conf
    • Kanki, T.; Klionsky, D.; Okamoto, K. Mitochondria autophagy in yeast. CORD Conf. Proc. 2011, 14, 1989–2001.
    • (2011) Proc , vol.14 , pp. 1989-2001
    • Kanki, T.1    Klionsky, D.2    Okamoto, K.3
  • 156
    • 82255192465 scopus 로고    scopus 로고
    • Degradation of paternal mitochondria by fertilization-triggered autophagy in C. Elegans embryos
    • Sato, M.; Sato, K. Degradation of paternal mitochondria by fertilization-triggered autophagy in C. elegans embryos. Science 2011, 334, 1141–1144.
    • (2011) Science , vol.334 , pp. 1141-1144
    • Sato, M.1    Sato, K.2
  • 158
    • 84925940926 scopus 로고    scopus 로고
    • PINK1 and Parkin—Mitochondrial interplay between phosphorylation and ubiquitylation in Parkinson’s disease
    • Kazlauskaite, A.; Muqit, M.M. PINK1 and Parkin—Mitochondrial interplay between phosphorylation and ubiquitylation in Parkinson’s disease. FEBS J. 2015, 282, 215–223.
    • (2015) FEBS J , vol.282 , pp. 215-223
    • Kazlauskaite, A.1    Muqit, M.M.2
  • 159
    • 84940723006 scopus 로고    scopus 로고
    • Molecular mechanisms underlying PINK1 and Parkin catalyzed ubiquitylation of substrates on damaged mitochondria
    • Koyano, F.; Matsuda, N. Molecular mechanisms underlying PINK1 and Parkin catalyzed ubiquitylation of substrates on damaged mitochondria. Biochim. Biophys. Acta 2015, 1853, 2791–2796.
    • (2015) Biochim. Biophys. Acta , vol.1853 , pp. 2791-2796
    • Koyano, F.1    Matsuda, N.2
  • 160
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra, D.; Tanaka, A.; Suen, D.F.; Youle, R.J. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 2008, 183, 795–803.
    • (2008) J. Cell Biol. , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 162
    • 77951181836 scopus 로고    scopus 로고
    • PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
    • Matsuda, N.; Sato, S.; Shiba, K.; Okatsu, K.; Saisho, K.; Gautier, C.A.; Sou, Y.S.; Saiki, S.; Kawajiri, S.; Sato, F., et al. PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy. J. Cell Biol. 2010, 189, 211–221.
    • (2010) J. Cell Biol , vol.189 , pp. 211-221
    • Matsuda, N.1    Sato, S.2    Shiba, K.3    Okatsu, K.4    Saisho, K.5    Gautier, C.A.6    Sou, Y.S.7    Saiki, S.8    Kawajiri, S.9    Sato, F.10
  • 165
    • 84871891737 scopus 로고    scopus 로고
    • PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of parkin and regulates mitophagy
    • Shiba-Fukushima, K.; Imai, Y.; Yoshida, S.; Ishihama, Y.; Kanao, T.; Sato, S.; Hattori, N. PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of parkin and regulates mitophagy. Sci. Rep. 2012, 2, 1002.
    • (2012) Sci. Rep. , vol.2 , pp. 1002
    • Shiba-Fukushima, K.1    Imai, Y.2    Yoshida, S.3    Ishihama, Y.4    Kanao, T.5    Sato, S.6    Hattori, N.7
  • 172
    • 79952424287 scopus 로고    scopus 로고
    • Tbc proteins: GAPs for mammalian small GTPase Rab?
    • Fukuda, M. Tbc proteins: GAPs for mammalian small GTPase Rab? Biosci. Rep. 2011, 31, 159–168.
    • (2011) Biosci. Rep. , vol.31 , pp. 159-168
    • Fukuda, M.1
  • 173
    • 0034676096 scopus 로고    scopus 로고
    • Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p
    • Mozdy, A.D.; McCaffery, J.M.; Shaw, J.M. Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J. Cell Biol. 2000, 151, 367–380.
    • (2000) J. Cell Biol , vol.151 , pp. 367-380
    • Mozdy, A.D.1    McCaffery, J.M.2    Shaw, J.M.3
  • 174
    • 0242579164 scopus 로고    scopus 로고
    • The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle
    • Suzuki, M.; Jeong, S.Y.; Karbowski, M.; Youle, R.J.; Tjandra, N. The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle. J. Mol. Biol. 2003, 334, 445–458.
    • (2003) J. Mol. Biol , vol.334 , pp. 445-458
    • Suzuki, M.1    Jeong, S.Y.2    Karbowski, M.3    Youle, R.J.4    Tjandra, N.5
  • 176
    • 84870995648 scopus 로고    scopus 로고
    • Regulation of lipid stores and metabolism by lipophagy
    • Liu, K.; Czaja, M.J. Regulation of lipid stores and metabolism by lipophagy. Cell Death Differ. 2013, 20, 3–11.
    • (2013) Cell Death Differ , vol.20 , pp. 3-11
    • Liu, K.1    Czaja, M.J.2
  • 180
    • 68849112456 scopus 로고    scopus 로고
    • Intermediate filaments: Primary determinants of cell architecture and plasticity
    • Herrmann, H.; Strelkov, S.V.; Burkhard, P.; Aebi, U. Intermediate filaments: Primary determinants of cell architecture and plasticity. J. Clin. Investig. 2009, 119, 1772–1783.
    • (2009) J. Clin. Investig , vol.119 , pp. 1772-1783
    • Herrmann, H.1    Strelkov, S.V.2    Burkhard, P.3    Aebi, U.4
  • 182
  • 183
    • 59449108978 scopus 로고    scopus 로고
    • Intermediate vimentin filaments and their role in intracellular organelle distribution
    • Minin, A.A.; Moldaver, M.N. Intermediate vimentin filaments and their role in intracellular organelle distribution. Biochemistry (Mosc.) 2008, 73, 1453–1466.
    • (2008) Biochemistry (Mosc.) , vol.73 , pp. 1453-1466
    • Minin, A.A.1    Moldaver, M.N.2
  • 184
    • 17444383492 scopus 로고    scopus 로고
    • Intermediate filaments and vesicular membrane traffic: The odd couple’s first dance?
    • Styers, M.L.; Kowalczyk, A.P.; Faundez, V. Intermediate filaments and vesicular membrane traffic: The odd couple’s first dance? Traffic 2005, 6, 359–365.
    • (2005) Traffic , vol.6 , pp. 359-365
    • Styers, M.L.1    Kowalczyk, A.P.2    Faundez, V.3
  • 185
    • 34249697100 scopus 로고    scopus 로고
    • Muscle intermediate filaments and their links to membranes and membranous organelles
    • Capetanaki, Y.; Bloch, R.J.; Kouloumenta, A.; Mavroidis, M.; Psarras, S. Muscle intermediate filaments and their links to membranes and membranous organelles. Exp. Cell Res. 2007, 313, 2063–2076.
    • (2007) Exp. Cell Res. , vol.313 , pp. 2063-2076
    • Capetanaki, Y.1    Bloch, R.J.2    Kouloumenta, A.3    Mavroidis, M.4    Psarras, S.5
  • 187
    • 85050577557 scopus 로고    scopus 로고
    • Role of intermediate filaments in vesicular traffic
    • Margiotta, A.; Bucci, C. Role of intermediate filaments in vesicular traffic. Cells 2016, 5, 20.
    • (2016) Cells , vol.5 , pp. 20
    • Margiotta, A.1    Bucci, C.2
  • 188
    • 9444239263 scopus 로고    scopus 로고
    • The endo-lysosomal sorting machinery interacts with the intermediate filament cytoskeleton
    • Styers, M.L.; Salazar, G.; Love, R.; Peden, A.A.; Kowalczyk, A.P.; Faundez, V. The endo-lysosomal sorting machinery interacts with the intermediate filament cytoskeleton. Mol. Biol. Cell 2004, 15, 5369–5382.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5369-5382
    • Styers, M.L.1    Salazar, G.2    Love, R.3    Peden, A.A.4    Kowalczyk, A.P.5    Faundez, V.6
  • 189
    • 84878831020 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth type 2b disease-causing Rab7a mutant proteins show altered interaction with the neuronal intermediate filament peripherin
    • Cogli, L.; Progida, C.; Thomas, C.L.; Spencer-Dene, B.; Donno, C.; Schiavo, G.; Bucci, C. Charcot-Marie-Tooth type 2b disease-causing Rab7a mutant proteins show altered interaction with the neuronal intermediate filament peripherin. Acta Neuropathol. 2013, 25, 257–272.
    • (2013) Acta Neuropathol. , vol.25 , pp. 257-272
    • Cogli, L.1    Progida, C.2    Thomas, C.L.3    Spencer-Dene, B.4    Donno, C.5    Schiavo, G.6    Bucci, C.7
  • 190
    • 84875641789 scopus 로고    scopus 로고
    • Vimentin phosphorylation and assembly are regulated by the small GTPase Rab7a
    • Cogli, L.; Progida, C.; Bramato, R.; Bucci, C. Vimentin phosphorylation and assembly are regulated by the small GTPase Rab7a. Biochim. Biophys. Acta 2013, 1833, 1283–1293.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 1283-1293
    • Cogli, L.1    Progida, C.2    Bramato, R.3    Bucci, C.4
  • 191
    • 84951027295 scopus 로고    scopus 로고
    • Rab7 regulates CDH1 endocytosis, circular dorsal ruffles genesis and thyroglobulin internalization in a thyroid cell line
    • Mascia, A.; Gentile, F.; Izzo, A.; Mollo, N.; De Luca, M.; Bucci, C.; Nitsch, L.; Calì, G. Rab7 regulates CDH1 endocytosis, circular dorsal ruffles genesis and thyroglobulin internalization in a thyroid cell line. J. Cell Physiol. 2016, 231, 1695–1708.
    • (2016) J. Cell Physiol , vol.231 , pp. 1695-1708
    • Mascia, A.1    Gentile, F.2    Izzo, A.3    Mollo, N.4    De Luca, M.5    Bucci, C.6    Nitsch, L.7    Calì, G.8
  • 194
    • 25444511328 scopus 로고    scopus 로고
    • Possible role of direct Rac1-Rab7 interaction in ruffled border formation of osteoclasts
    • Sun, Y.; Buki, K.G.; Ettala, O.; Vaaraniemi, J.P.; Vaananen, H.K. Possible role of direct Rac1-Rab7 interaction in ruffled border formation of osteoclasts. J. Biol. Chem. 2005, 280, 32356–32361.
    • (2005) J. Biol. Chem , vol.280 , pp. 32356-32361
    • Sun, Y.1    Buki, K.G.2    Ettala, O.3    Vaaraniemi, J.P.4    Vaananen, H.K.5
  • 195
    • 67449147361 scopus 로고    scopus 로고
    • Rab7 activation by growth factor withdrawal contributes to the induction of apoptosis
    • Romero Rosales, K.; Peralta, E.R.; Guenther, G.G.; Wong, S.Y.; Edinger, A.L. Rab7 activation by growth factor withdrawal contributes to the induction of apoptosis. Mol. Biol. Cell 2009, 20, 2831–2840.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2831-2840
    • Romero Rosales, K.1    Peralta, E.R.2    Guenther, G.G.3    Wong, S.Y.4    Edinger, A.L.5
  • 196
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • Hanahan, D.; Weinberg, R.A. Hallmarks of cancer: The next generation. Cell 2011, 144, 646–674.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 197
    • 84863115707 scopus 로고    scopus 로고
    • A role of Rab7 in stabilizing EGFR-HER2 and in sustaining Akt survival signal
    • Wang, T.; Zhang, M.; Ma, Z.; Guo, K.; Tergaonkar, V.; Zeng, Q.; Hong, W. A role of Rab7 in stabilizing EGFR-HER2 and in sustaining Akt survival signal. J. Cell. Physiol 2012, 227, 2788–2797.
    • (2012) J. Cell. Physiol , vol.227 , pp. 2788-2797
    • Wang, T.1    Zhang, M.2    Ma, Z.3    Guo, K.4    Tergaonkar, V.5    Zeng, Q.6    Hong, W.7
  • 198
    • 83355166955 scopus 로고    scopus 로고
    • Phosphorylation of membrane type 1-matrix metalloproteinase (Mt1-mmp) and its vesicle-associated membrane protein 7 (Vamp7)-dependent trafficking facilitate cell invasion and migration
    • Williams, K.C.; Coppolino, M.G. Phosphorylation of membrane type 1-matrix metalloproteinase (mt1-mmp) and its vesicle-associated membrane protein 7 (Vamp7)-dependent trafficking facilitate cell invasion and migration. J. Biol. Chem. 2011, 286, 43405–43416.
    • (2011) J. Biol. Chem , vol.286 , pp. 43405-43416
    • Williams, K.C.1    Coppolino, M.G.2
  • 200
    • 73549084068 scopus 로고    scopus 로고
    • Thiazolidinediones induce Rab7-RILP-MAPK-dependent juxtanuclear lysosome aggregation and reduce tumor cell invasion
    • Steffan, J.J.; Cardelli, J.A. Thiazolidinediones induce Rab7-RILP-MAPK-dependent juxtanuclear lysosome aggregation and reduce tumor cell invasion. Traffic 2010, 11, 274–286.
    • (2010) Traffic , vol.11 , pp. 274-286
    • Steffan, J.J.1    Cardelli, J.A.2
  • 202
    • 0038049137 scopus 로고    scopus 로고
    • Tumor-cell invasion and migration: Diversity and escape mechanisms
    • Friedl, P.; Wolf, K. Tumor-cell invasion and migration: Diversity and escape mechanisms. Nat. Rev. Cancer 2003, 3, 362–374.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 362-374
    • Friedl, P.1    Wolf, K.2
  • 203
    • 54749146365 scopus 로고    scopus 로고
    • Tube travel: The role of proteases in individual and collective cancer cell invasion
    • Friedl, P.; Wolf, K. Tube travel: The role of proteases in individual and collective cancer cell invasion. Cancer Res. 2008, 68, 7247–7249.
    • (2008) Cancer Res , vol.68 , pp. 7247-7249
    • Friedl, P.1    Wolf, K.2
  • 204
    • 0001295227 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor modulators as potential chemopreventive agents. Mol
    • Kopelovich, L.; Fay, J.R.; Glazer, R.I.; Crowell, J.A. Peroxisome proliferator-activated receptor modulators as potential chemopreventive agents. Mol. Cancer Ther. 2002, 1, 357–363.
    • (2002) Cancer Ther , vol.1 , pp. 357-363
    • Kopelovich, L.1    Fay, J.R.2    Glazer, R.I.3    Crowell, J.A.4
  • 205
    • 77951165622 scopus 로고    scopus 로고
    • Hgf-induced invasion by prostate tumor cells requires anterograde lysosome trafficking and activity of Na+-H+ exchangers
    • Steffan, J.J.; Williams, B.C.; Welbourne, T.; Cardelli, J.A. Hgf-induced invasion by prostate tumor cells requires anterograde lysosome trafficking and activity of Na+-H+ exchangers. J. Cell Sci. 2010, 123, 1151–1159.
    • (2010) J. Cell Sci. , vol.123 , pp. 1151-1159
    • Steffan, J.J.1    Williams, B.C.2    Welbourne, T.3    Cardelli, J.A.4
  • 206
    • 34848855124 scopus 로고    scopus 로고
    • The MET receptor tyrosine kinase in invasion and metastasis
    • Benvenuti, S.; Comoglio, P.M. The MET receptor tyrosine kinase in invasion and metastasis. J. Cell. Physiol. 2007, 213, 316–325.
    • (2007) J. Cell. Physiol , vol.213 , pp. 316-325
    • Benvenuti, S.1    Comoglio, P.M.2
  • 207
    • 34247874425 scopus 로고    scopus 로고
    • Involvement of Rabring7 in EGF receptor degradation as an E3 ligase. Biochem. Biophys. Res
    • Sakane, A.; Hatakeyama, S.; Sasaki, T. Involvement of Rabring7 in EGF receptor degradation as an E3 ligase. Biochem. Biophys. Res. Commun. 2007, 357, 1058–1064.
    • (2007) Commun , vol.357 , pp. 1058-1064
    • Sakane, A.1    Hatakeyama, S.2    Sasaki, T.3
  • 211
    • 84957991211 scopus 로고    scopus 로고
    • PTEN modulates EGFR late endocytic trafficking and degradation by dephosphorylating Rab7
    • Shinde, S.R.; Maddika, S. PTEN modulates EGFR late endocytic trafficking and degradation by dephosphorylating Rab7. Nat. Commun. 2016, 7, 10689.
    • (2016) Nat. Commun. , vol.7 , pp. 10689
    • Shinde, S.R.1    Maddika, S.2
  • 215
    • 33750728621 scopus 로고    scopus 로고
    • Protrudin induces neurite formation by directional membrane trafficking
    • Shirane, M.; Nakayama, K.I. Protrudin induces neurite formation by directional membrane trafficking. Science 2006, 314, 818–821.
    • (2006) Science , vol.314 , pp. 818-821
    • Shirane, M.1    Nakayama, K.I.2
  • 216
    • 77955956961 scopus 로고    scopus 로고
    • Rab GTPases-dependent endocytic pathways regulate neuronal migration and maturation through n-cadherin trafficking
    • Kawauchi, T.; Sekine, K.; Shikanai, M.; Chihama, K.; Tomita, K.; Kubo, K.; Nakajima, K.; Nabeshima, Y.; Hoshino, M. Rab GTPases-dependent endocytic pathways regulate neuronal migration and maturation through n-cadherin trafficking. Neuron 2010, 67, 588–602.
    • (2010) Neuron , vol.67 , pp. 588-602
    • Kawauchi, T.1    Sekine, K.2    Shikanai, M.3    Chihama, K.4    Tomita, K.5    Kubo, K.6    Nakajima, K.7    Nabeshima, Y.8    Hoshino, M.9
  • 217
    • 84869885373 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease and intracellular traffic
    • Bucci, C.; Bakke, O.; Progida, C. Charcot-Marie-Tooth disease and intracellular traffic. Prog Neurobiol 2012, 99, 191–225.
    • (2012) Prog Neurobiol , vol.99 , pp. 191-225
    • Bucci, C.1    Bakke, O.2    Progida, C.3
  • 218
    • 44649154996 scopus 로고    scopus 로고
    • Characterization of the Rab7K157N mutant protein associated with Charcot-Marie-Tooth type 2b. Biochem. Biophys. Res
    • De Luca, A.; Progida, C.; Spinosa, M.R.; Alifano, P.; Bucci, C. Characterization of the Rab7K157N mutant protein associated with Charcot-Marie-Tooth type 2b. Biochem. Biophys. Res. Commun. 2008, 372, 283–287.
    • (2008) Commun , vol.372 , pp. 283-287
    • De Luca, A.1    Progida, C.2    Spinosa, M.R.3    Alifano, P.4    Bucci, C.5
  • 219
    • 39549098329 scopus 로고    scopus 로고
    • Functional characterization of Rab7 mutant proteins associated with Charcot-Marie-Tooth type 2b disease
    • Spinosa, M.R.; Progida, C.; De Luca, A.; Colucci, A.M.R.; Alifano, P.; Bucci, C. Functional characterization of Rab7 mutant proteins associated with Charcot-Marie-Tooth type 2b disease. J. Neurosci. 2008, 28, 1640–1648.
    • (2008) J. Neurosci , vol.28 , pp. 1640-1648
    • Spinosa, M.R.1    Progida, C.2    De Luca, A.3    Colucci, A.M.R.4    Alifano, P.5    Bucci, C.6
  • 220
    • 77950686629 scopus 로고    scopus 로고
    • Disease mutations in rab7 result in unregulated nucleotide exchange and inappropriate activation
    • McCray, B.A.; Skordalakes, E.; Taylor, J.P. Disease mutations in rab7 result in unregulated nucleotide exchange and inappropriate activation. Hum. Mol. Genet. 2010, 19, 1033–1047.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 1033-1047
    • McCray, B.A.1    Skordalakes, E.2    Taylor, J.P.3
  • 222
    • 78149353040 scopus 로고    scopus 로고
    • The mood stabilizer valproic acid improves defective neurite formation caused by Charcot-Marie-Tooth disease-associated mutant Rab7 through the JNK signaling pathway
    • Yamauchi, J.; Torii, T.; Kusakawa, S.; Sanbe, A.; Nakamura, K.; Takashima, S.; Hamasaki, H.; Kawaguchi, S.; Miyamoto, Y.; Tanoue, A. The mood stabilizer valproic acid improves defective neurite formation caused by Charcot-Marie-Tooth disease-associated mutant Rab7 through the JNK signaling pathway. J. Neurosci. Res. 2010, 88, 3189–3197.
    • (2010) J. Neurosci. Res , vol.88 , pp. 3189-3197
    • Yamauchi, J.1    Torii, T.2    Kusakawa, S.3    Sanbe, A.4    Nakamura, K.5    Takashima, S.6    Hamasaki, H.7    Kawaguchi, S.8    Miyamoto, Y.9    Tanoue, A.10
  • 224
    • 0023785951 scopus 로고
    • Relationship between the nerve growth factor-regulated clone 73 gene product and the 58-kilodalton neuronal intermediate filament protein (Peripherin)
    • Aletta, J.M.; Angeletti, R.; Liem, R.K.; Purcell, C.; Shelanski, M.L.; Greene, L.A. Relationship between the nerve growth factor-regulated clone 73 gene product and the 58-kilodalton neuronal intermediate filament protein (peripherin). J. Neurochem. 1988, 51, 1317–1320.
    • (1988) J. Neurochem , vol.51 , pp. 1317-1320
    • Aletta, J.M.1    Angeletti, R.2    Liem, R.K.3    Purcell, C.4    Shelanski, M.L.5    Greene, L.A.6
  • 225
    • 77953616305 scopus 로고    scopus 로고
    • Intermediate filament peripherin inhibits neuritogenesis in type ii spiral ganglion neurons in vitro
    • Barclay, M.; Julien, J.P.; Ryan, A.F.; Housley, G.D. Type III intermediate filament peripherin inhibits neuritogenesis in type ii spiral ganglion neurons in vitro. Neurosci. Lett. 2010, 478, 51–55.
    • (2010) Neurosci. Lett. , vol.478 , pp. 51-55
    • Barclay, M.1    Julien, J.P.2    Ryan, A.F.3    Housley, G.D.4    Type, I.5
  • 227
    • 43949137907 scopus 로고    scopus 로고
    • Neuronal intermediate filament expression in rat dorsal root ganglia sensory neurons: An in vivo and in vitro study
    • Fornaro, M.; Lee, J.M.; Raimondo, S.; Nicolino, S.; Geuna, S.; Giacobini-Robecchi, M. Neuronal intermediate filament expression in rat dorsal root ganglia sensory neurons: An in vivo and in vitro study. Neuroscience 2008, 153, 1153–1163.
    • (2008) Neuroscience , vol.153 , pp. 1153-1163
    • Fornaro, M.1    Lee, J.M.2    Raimondo, S.3    Nicolino, S.4    Geuna, S.5    Giacobini-Robecchi, M.6
  • 228
    • 0344875476 scopus 로고    scopus 로고
    • A role for intermediate filaments in determining and maintaining the shape of nerve cells
    • Helfand, B.T.; Mendez, M.G.; Pugh, J.; Delsert, C.; Goldman, R.D. A role for intermediate filaments in determining and maintaining the shape of nerve cells. Mol. Biol. Cell 2003, 14, 5069–5081.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 5069-5081
    • Helfand, B.T.1    Mendez, M.G.2    Pugh, J.3    Delsert, C.4    Goldman, R.D.5
  • 230
    • 0024305705 scopus 로고
    • Structure of the gene encoding peripherin, an NGF-regulated neuronal-specific type III intermediate filament protein
    • Thompson, M.A.; Ziff, E.B. Structure of the gene encoding peripherin, an NGF-regulated neuronal-specific type III intermediate filament protein. Neuron 1989, 2, 1043–1053.
    • (1989) Neuron , vol.2 , pp. 1043-1053
    • Thompson, M.A.1    Ziff, E.B.2
  • 231
    • 0033230327 scopus 로고    scopus 로고
    • Late onset of motor neurons in mice overexpressing wild-type peripherin
    • Beaulieu, J.M.; Nguyen, M.D.; Julien, J.P. Late onset of motor neurons in mice overexpressing wild-type peripherin. J. Cell Biol. 1999, 147, 531–544.
    • (1999) J. Cell Biol , vol.147 , pp. 531-544
    • Beaulieu, J.M.1    Nguyen, M.D.2    Julien, J.P.3
  • 232
    • 84866155363 scopus 로고    scopus 로고
    • Neuronal autophagy: A housekeeper or a fighter in neuronal cell survival? Exp
    • Lee, J.A. Neuronal autophagy: A housekeeper or a fighter in neuronal cell survival? Exp. Neurobiol. 2012, 21, 1–8.
    • (2012) Neurobiol. , vol.21 , pp. 1-8
    • Lee, J.A.1
  • 233
    • 33745913017 scopus 로고    scopus 로고
    • Defective axonal transport of neurofilament proteins in neurons overexpressing peripherin
    • Millecamps, S.; Robertson, J.; Lariviere, R.; Mallet, J.; Julien, J.P. Defective axonal transport of neurofilament proteins in neurons overexpressing peripherin. J. Neurochem. 2006, 98, 926–938.
    • (2006) J. Neurochem , vol.98 , pp. 926-938
    • Millecamps, S.1    Robertson, J.2    Lariviere, R.3    Mallet, J.4    Julien, J.P.5
  • 234
    • 0030797216 scopus 로고    scopus 로고
    • Endocytic pathway from the basal plasma membrane to the ruffled border membrane in bone-resorbing osteoclasts
    • Palokangas, H.; Mulari, M.; Väänänen, H.K. Endocytic pathway from the basal plasma membrane to the ruffled border membrane in bone-resorbing osteoclasts. J. Cell Sci. 1997, 110, 1767–1780.
    • (1997) J. Cell Sci , vol.110 , pp. 1767-1780
    • Palokangas, H.1    Mulari, M.2    Väänänen, H.K.3
  • 235
    • 0035914465 scopus 로고    scopus 로고
    • Downregulation of small GTPase Rab7 impairs osteoclast polarization and bone resorption
    • Zhao, H.; Laitala-Leinonen, T.; Parikka, V.; Väänänen, H.K. Downregulation of small GTPase Rab7 impairs osteoclast polarization and bone resorption. J. Biol. Chem. 2001, 276, 39295–39302.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39295-39302
    • Zhao, H.1    Laitala-Leinonen, T.2    Parikka, V.3    Väänänen, H.K.4
  • 236
    • 84943201622 scopus 로고    scopus 로고
    • Rab7a and Rab27b control secretion of endothelial microrna through extracellular vesicles
    • Jaé, N.; McEwan, D.G.; Manavski, Y.; Boon, R.A.; Dimmeler, S. Rab7a and Rab27b control secretion of endothelial microrna through extracellular vesicles. FEBS Lett. 2015, 589, 3182–3188.
    • (2015) FEBS Lett , vol.589 , pp. 3182-3188
    • Jaé, N.1    McEwan, D.G.2    Manavski, Y.3    Boon, R.A.4    Dimmeler, S.5
  • 239
    • 84929485159 scopus 로고    scopus 로고
    • McNiven, M.A. Hbv secretion is regulated through the activation of endocytic and autophagic compartments mediated by Rab7 stimulation
    • Inoue, J.; Krueger, E.W.; Chen, J.; Cao, H.; Ninomiya, M.; McNiven, M.A. Hbv secretion is regulated through the activation of endocytic and autophagic compartments mediated by Rab7 stimulation. J. Cell Sci. 2015, 128, 1696–1706.
    • (2015) J. Cell Sci , vol.128 , pp. 1696-1706
    • Inoue, J.1    Krueger, E.W.2    Chen, J.3    Cao, H.4    Ninomiya, M.5
  • 240
  • 241
    • 84896363994 scopus 로고    scopus 로고
    • Overexpression of a vesicle trafficking gene, Osrab7, enhances salt tolerance in rice
    • Peng, X.; Ding, X.; Chang, T.; Wang, Z.; Liu, R.; Zeng, X.; Cai, Y.; Zhu, Y. Overexpression of a vesicle trafficking gene, Osrab7, enhances salt tolerance in rice. Sci. World J. 2014, 2014, 483526.
    • (2014) Sci. World J. , vol.2014 , pp. 483526
    • Peng, X.1    Ding, X.2    Chang, T.3    Wang, Z.4    Liu, R.5    Zeng, X.6    Cai, Y.7    Zhu, Y.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.