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Volumn 127, Issue 12, 2014, Pages 2697-2708

RILP regulates vacuolar ATPase through interaction with the V1G1 subunit

Author keywords

Rab7; RILP; Ubiquitin; V1G1; Vacuolar ATPase

Indexed keywords

ADENOSINE TRIPHOSPHATASE; PROTEIN; PROTEIN V1G1; RAB INTERACTING LYSOSOMAL PROTEIN; RAB7 PROTEIN; UNCLASSIFIED DRUG; VACUOLAR ADENOSINE TRIPHOSPHATASE; ATP6V1G1 PROTEIN, HUMAN; DYNACTIN; MICROTUBULE ASSOCIATED PROTEIN; PROTEASOME; PROTEIN BINDING; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; RAB PROTEIN; RILP PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 84902477498     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.142604     Document Type: Article
Times cited : (57)

References (62)
  • 1
    • 84879768677 scopus 로고    scopus 로고
    • Rab GTPases-cargo direct interactions: fine modulators of intracellular trafficking
    • Aloisi, A. L. and Bucci, C. (2013). Rab GTPases-cargo direct interactions: fine modulators of intracellular trafficking. Histol. Histopathol. 28, 839-849.
    • (2013) Histol. Histopathol. , vol.28 , pp. 839-849
    • Aloisi, A.L.1    Bucci, C.2
  • 2
    • 0029869843 scopus 로고    scopus 로고
    • An endosomal b COP is involved in the pH-dependent formation of transport vesicles destined for late endosomes
    • Aniento, F., Gu, F., Parton, R. G. and Gruenberg, J. (1996). An endosomal b COP is involved in the pH-dependent formation of transport vesicles destined for late endosomes. J. Cell Biol. 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
  • 4
    • 0027255909 scopus 로고
    • Elimination of false positives that arise in using the two-hybrid system
    • Bartel, P., Chien, C. T., Sternglanz, R. and Fields, S. (1993). Elimination of false positives that arise in using the two-hybrid system. Biotechniques 14, 920-924.
    • (1993) Biotechniques , vol.14 , pp. 920-924
    • Bartel, P.1    Chien, C.T.2    Sternglanz, R.3    Fields, S.4
  • 5
    • 26444562441 scopus 로고    scopus 로고
    • Signal transduction gRABs attention
    • Bucci, C. and Chiariello, M. (2006). Signal transduction gRABs attention. Cell. Signal. 18, 1-8.
    • (2006) Cell. Signal. , vol.18 , pp. 1-8
    • Bucci, C.1    Chiariello, M.2
  • 7
    • 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. and Zerial, M. (1992). The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway. Cell 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
  • 9
    • 0035865135 scopus 로고    scopus 로고
    • Rabinteracting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes
    • Cantalupo, G., Alifano, P., Roberti, V., Bruni, C. B. and Bucci, C. (2001). Rabinteracting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes. EMBO J. 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
  • 11
    • 0025363426 scopus 로고
    • Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments
    • Chavrier, P., Parton, R. G., Hauri, H. P., Simons, K. and Zerial, M. (1990). Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments. Cell 62, 317-329.
    • (1990) Cell , vol.62 , pp. 317-329
    • Chavrier, P.1    Parton, R.G.2    Hauri, H.P.3    Simons, K.4    Zerial, M.5
  • 12
    • 0032810862 scopus 로고    scopus 로고
    • The small GTPases Rab5a, Rab5b and Rab5c are differentially phosphorylated in vitro
    • Chiariello, M., Bruni, C. B. and Bucci, C. (1999). The small GTPases Rab5a, Rab5b and Rab5c are differentially phosphorylated in vitro. FEBS Lett. 453, 20-24.
    • (1999) FEBS Lett. , vol.453 , pp. 20-24
    • Chiariello, M.1    Bruni, C.B.2    Bucci, C.3
  • 14
    • 0028014372 scopus 로고
    • Vacuolar ATPase activity is required for endosomal carrier vesicle formation
    • Clague, M. J., Urbé, S., Aniento, F. and Gruenberg, J. (1994). Vacuolar ATPase activity is required for endosomal carrier vesicle formation. J. Biol. Chem. 269, 21-24.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21-24
    • Clague, M.J.1    Urbé, S.2    Aniento, F.3    Gruenberg, J.4
  • 15
    • 84875641789 scopus 로고    scopus 로고
    • Vimentin phosphorylation and assembly are regulated by the small GTPase Rab7a
    • Cogli, L., Progida, C., Bramato, R. and Bucci, C. (2013a). Vimentin phosphorylation and assembly are regulated by the small GTPase Rab7a. Biochim. Biophys. Acta 1833, 1283-1293.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 1283-1293
    • Cogli, L.1    Progida, C.2    Bramato, R.3    Bucci, C.4
  • 16
    • 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. and Bucci, C. (2013b). Charcot-Marie-Tooth type 2B disease-causing RAB7A mutant proteins show altered interaction with the neuronal intermediate filament peripherin. Acta Neuropathol. 125, 257-272.
    • (2013) Acta Neuropathol. , vol.125 , 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
  • 17
    • 22144477960 scopus 로고    scopus 로고
    • The Rab-interacting lysosomal protein, a Rab7 and Rab34 effector, is capable of self-interaction
    • Colucci, A. M. R., Campana, M. C., Bellopede, M. and Bucci, C. (2005a). The Rab-interacting lysosomal protein, a Rab7 and Rab34 effector, is capable of self-interaction. Biochem. Biophys. Res. Commun. 334, 128-133.
    • (2005) Biochem. Biophys. Res. Commun. , vol.334 , pp. 128-133
    • Colucci, A.M.R.1    Campana, M.C.2    Bellopede, M.3    Bucci, C.4
  • 18
    • 32344452495 scopus 로고    scopus 로고
    • Expression, assay, and functional properties of RILP
    • Colucci, A. M. R., Spinosa, M. R. and Bucci, C. (2005b). Expression, assay, and functional properties of RILP. Methods Enzymol. 403, 664-675.
    • (2005) Methods Enzymol. , vol.403 , pp. 664-675
    • Colucci, A.M.R.1    Spinosa, M.R.2    Bucci, C.3
  • 19
    • 0000241799 scopus 로고
    • pH and the recycling of transferrin during receptor-mediated endocytosis
    • Dautry-Varsat, A., Ciechanover, A. and Lodish, H. F. (1983). pH and the recycling of transferrin during receptor-mediated endocytosis. Proc. Natl. Acad. Sci. USA 80, 2258-2262.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2258-2262
    • Dautry-Varsat, A.1    Ciechanover, A.2    Lodish, H.F.3
  • 20
    • 44649154996 scopus 로고    scopus 로고
    • Characterization of the Rab7K157N mutant protein associated with Charcot-Marie-Tooth type 2B
    • De Luca, A., Progida, C., Spinosa, M. R., Alifano, P. and Bucci, C. (2008). Characterization of the Rab7K157N mutant protein associated with Charcot-Marie-Tooth type 2B. Biochem. Biophys. Res. Commun. 372, 283-287.
    • (2008) Biochem. Biophys. Res. Commun. , vol.372 , pp. 283-287
    • De Luca, A.1    Progida, C.2    Spinosa, M.R.3    Alifano, P.4    Bucci, C.5
  • 21
    • 77954909378 scopus 로고    scopus 로고
    • Regulation of V-ATPase activity and assembly by extracellular pH
    • Diakov, T. T. and Kane, P. M. (2010). Regulation of V-ATPase activity and assembly by extracellular pH. J. Biol. Chem. 285, 23771-23778.
    • (2010) J. Biol. Chem. , vol.285 , pp. 23771-23778
    • Diakov, T.T.1    Kane, P.M.2
  • 22
    • 79955005373 scopus 로고    scopus 로고
    • A role for V-ATPase subunits in synaptic vesicle fusion?
    • El Far, O. and Seagar, M. (2011). A role for V-ATPase subunits in synaptic vesicle fusion? J. Neurochem. 117, 603-612.
    • (2011) J. Neurochem. , vol.117 , pp. 603-612
    • El Far, O.1    Seagar, M.2
  • 23
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology
    • Forgac, M. (2007). Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol. 8, 917-929.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 917-929
    • Forgac, M.1
  • 25
    • 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. E., Bucci, C., Vieira, O. V., Schroer, T. A. and Grinstein, S. (2003). Phagosomes fuse with late endosomes and/or lysosomes by extension of membrane protrusions along microtubules: role of Rab7 and RILP. Mol. Cell. Biol. 23, 6494-6506.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6494-6506
    • Harrison, R.E.1    Bucci, C.2    Vieira, O.V.3    Schroer, T.A.4    Grinstein, S.5
  • 27
    • 62149142874 scopus 로고    scopus 로고
    • V-ATPase functions in normal and disease processes
    • Hinton, A., Bond, S. and Forgac, M. (2009). V-ATPase functions in normal and disease processes. Pflugers Arch. 457, 589-598.
    • (2009) Pflugers Arch. , vol.457 , pp. 589-598
    • Hinton, A.1    Bond, S.2    Forgac, M.3
  • 28
    • 0020601856 scopus 로고
    • Internalization and processing of transferrin and the transferrin receptor in human carcinoma A431 cells
    • Hopkins, C. R. and Trowbridge, I. S. (1983). Internalization and processing of transferrin and the transferrin receptor in human carcinoma A431 cells. J. Cell Biol. 97, 508-521.
    • (1983) J. Cell Biol. , vol.97 , pp. 508-521
    • Hopkins, C.R.1    Trowbridge, I.S.2
  • 30
    • 33847003020 scopus 로고    scopus 로고
    • Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150Glued, ORP1L, and the receptor betalll spectrin
    • Johansson, M., Rocha, N., Zwart, W., Jordens, I., Janssen, L., Kuijl, C., Olkkonen, V. M. and Neefjes, J. (2007). Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150Glued, ORP1L, and the receptor betalll spectrin. J. Cell Biol. 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
  • 32
    • 33645119556 scopus 로고    scopus 로고
    • The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase
    • Kane, P. M. (2006). The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase. Microbiol. Mol. Biol. Rev. 70, 177-191.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 177-191
    • Kane, P.M.1
  • 33
    • 84860815342 scopus 로고    scopus 로고
    • Targeting reversible disassembly as a mechanism of controlling V-ATPase activity
    • Kane, P. M. (2012). Targeting reversible disassembly as a mechanism of controlling V-ATPase activity. Curr. Protein Pept. Sci. 13, 117-123.
    • (2012) Curr. Protein Pept. Sci. , vol.13 , pp. 117-123
    • Kane, P.M.1
  • 34
    • 0142089024 scopus 로고    scopus 로고
    • Assembly and regulation of the yeast vacuolar H+-ATPase
    • Kane, P. M. and Smardon, A. M. (2003). Assembly and regulation of the yeast vacuolar H+-ATPase. J. Bioenerg. Biomembr. 35, 313-321.
    • (2003) J. Bioenerg. Biomembr. , vol.35 , pp. 313-321
    • Kane, P.M.1    Smardon, A.M.2
  • 36
    • 84860813774 scopus 로고    scopus 로고
    • V-ATPase subunit interactions: the long road to therapeutic targeting
    • Kartner, N. and Manolson, M. F. (2012). V-ATPase subunit interactions: the long road to therapeutic targeting. Curr. Protein Pept. Sci. 13, 164-179.
    • (2012) Curr. Protein Pept. Sci. , vol.13 , pp. 164-179
    • Kartner, N.1    Manolson, M.F.2
  • 37
    • 47349120492 scopus 로고    scopus 로고
    • The V-type H+-ATPase in vesicular trafficking: targeting, regulation and function
    • Marshansky, V. and Futai, M. (2008). The V-type H+-ATPase in vesicular trafficking: targeting, regulation and function. Curr. Opin. Cell Biol. 20, 415-426.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 415-426
    • Marshansky, V.1    Futai, M.2
  • 38
    • 0037184028 scopus 로고    scopus 로고
    • Differential localization of the vacuolar H+ pump with G subunit isoforms (G1 and G2) in mouse neurons
    • Murata, Y., Sun-Wada, G. H., Yoshimizu, T., Yamamoto, A., Wada, Y. and Futai, M. (2002). Differential localization of the vacuolar H+ pump with G subunit isoforms (G1 and G2) in mouse neurons. J. Biol. Chem. 277, 36296-36303.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36296-36303
    • Murata, Y.1    Sun-Wada, G.H.2    Yoshimizu, T.3    Yamamoto, A.4    Wada, Y.5    Futai, M.6
  • 39
    • 84857219068 scopus 로고    scopus 로고
    • The Rab21-GEF activity of Varp, but not its Rab32/38 effector function, is required for dendrite formation in melanocytes
    • Ohbayashi, N., Yatsu, A., Tamura, K. and Fukuda, M. (2012). The Rab21-GEF activity of Varp, but not its Rab32/38 effector function, is required for dendrite formation in melanocytes. Mol. Biol. Cell 23, 669-678.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 669-678
    • Ohbayashi, N.1    Yatsu, A.2    Tamura, K.3    Fukuda, M.4
  • 40
    • 33747371955 scopus 로고    scopus 로고
    • The E and G subunits of the yeast V-ATPase interact tightly and are both present at more than one copy per V1 complex
    • Ohira, M., Smardon, A. M., Charsky, C. M., Liu, J., Tarsio, M. and Kane, P. M. (2006). The E and G subunits of the yeast V-ATPase interact tightly and are both present at more than one copy per V1 complex. J. Biol. Chem. 281, 22752-22760.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22752-22760
    • Ohira, M.1    Smardon, A.M.2    Charsky, C.M.3    Liu, J.4    Tarsio, M.5    Kane, P.M.6
  • 44
    • 36549019071 scopus 로고    scopus 로고
    • RILP is required for the proper morphology and function of late endosomes
    • Progida, C., Malerød, L., Stuffers, S., Brech, A., Bucci, C. and Stenmark, H. (2007). RILP is required for the proper morphology and function of late endosomes. J. Cell Sci. 120, 3729-3737.
    • (2007) J. Cell Sci. , vol.120 , pp. 3729-3737
    • Progida, C.1    Malerød, L.2    Stuffers, S.3    Brech, A.4    Bucci, C.5    Stenmark, H.6
  • 46
    • 38349192768 scopus 로고    scopus 로고
    • The vacuolar (H+)-ATPase: subunit arrangement and in vivo regulation
    • Qi, J., Wang, Y. and Forgac, M. (2007). The vacuolar (H+)-ATPase: subunit arrangement and in vivo regulation. J. Bioenerg. Biomembr. 39, 423-426.
    • (2007) J. Bioenerg. Biomembr. , vol.39 , pp. 423-426
    • Qi, J.1    Wang, Y.2    Forgac, M.3
  • 47
    • 84860360983 scopus 로고    scopus 로고
    • V-ATPase, ScNhx1p and yeast vacuole fusion
    • Qiu, Q. S. (2012). V-ATPase, ScNhx1p and yeast vacuole fusion. J. Genet. Genomics 39, 167-171.
    • (2012) J. Genet. Genomics , vol.39 , pp. 167-171
    • Qiu, Q.S.1
  • 48
    • 70349470981 scopus 로고    scopus 로고
    • Dual degradation mechanisms ensure disposal of NHE6 mutant protein associated with neurological disease
    • Roxrud, I., Raiborg, C., Gilfillan, G. D., Strømme, P. and Stenmark, H. (2009). Dual degradation mechanisms ensure disposal of NHE6 mutant protein associated with neurological disease. Exp. Cell Res. 315, 3014-3027.
    • (2009) Exp. Cell Res. , vol.315 , pp. 3014-3027
    • Roxrud, I.1    Raiborg, C.2    Gilfillan, G.D.3    Strømme, P.4    Stenmark, H.5
  • 52
    • 0037134525 scopus 로고    scopus 로고
    • The RAVE complex is essential for stable assembly of the yeast V-ATPase
    • Smardon, A. M., Tarsio, M. and Kane, P. M. (2002). The RAVE complex is essential for stable assembly of the yeast V-ATPase. J. Biol. Chem. 277, 13831-13839.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13831-13839
    • Smardon, A.M.1    Tarsio, M.2    Kane, P.M.3
  • 53
    • 0033812944 scopus 로고    scopus 로고
    • Mutations in ATP6N1B, encoding a new kidney vacuolar proton pump 116-kD subunit, cause recessive distal renal tubular acidosis with preserved hearing
    • Smith, A. N., Skaug, J., Choate, K. A., Nayir, A., Bakkaloglu, A., Ozen, S., Hulton, S. A., Sanjad, S. A., Al-Sabban, E. A., Lifton, R. P. et al. (2000). Mutations in ATP6N1B, encoding a new kidney vacuolar proton pump 116-kD subunit, cause recessive distal renal tubular acidosis with preserved hearing. Nat. Genet. 26, 71-75.
    • (2000) Nat. Genet. , vol.26 , pp. 71-75
    • Smith, A.N.1    Skaug, J.2    Choate, K.A.3    Nayir, A.4    Bakkaloglu, A.5    Ozen, S.6    Hulton, S.A.7    Sanjad, S.A.8    Al-Sabban, E.A.9    Lifton, R.P.10
  • 54
    • 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. and Bucci, C. (2008). Functional characterization of Rab7 mutant proteins associated with Charcot-Marie-Tooth type 2B disease. J. Neurosci. 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
  • 55
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • Stenmark, H. (2009). Rab GTPases as coordinators of vesicle traffic. Nat. Rev. Mol. Cell Biol. 10, 513-525.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 56
    • 3542998744 scopus 로고    scopus 로고
    • Diverse and essential roles of mammalian vacuolar-type proton pump ATPase: toward the physiological understanding of inside acidic compartments
    • Sun-Wada, G. H., Wada, Y. and Futai, M. (2004). Diverse and essential roles of mammalian vacuolar-type proton pump ATPase: toward the physiological understanding of inside acidic compartments. Biochim. Biophys. Acta 1658, 106-114.
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 106-114
    • Sun-Wada, G.H.1    Wada, Y.2    Futai, M.3
  • 58
    • 77953255215 scopus 로고    scopus 로고
    • Regulation and isoform function of the V-ATPases
    • Toei, M., Saum, R. and Forgac, M. (2010). Regulation and isoform function of the V-ATPases. Biochemistry 49, 4715-4723.
    • (2010) Biochemistry , vol.49 , pp. 4715-4723
    • Toei, M.1    Saum, R.2    Forgac, M.3
  • 59
    • 0030611895 scopus 로고    scopus 로고
    • V1-situated stalk subunits of the yeast vacuolar protontranslocating ATPase
    • Tomashek, J. J., Graham, L. A., Hutchins, M. U., Stevens, T. H. and Klionsky, D. J. (1997). V1-situated stalk subunits of the yeast vacuolar protontranslocating ATPase. J. Biol. Chem. 272, 26787-26793.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26787-26793
    • Tomashek, J.J.1    Graham, L.A.2    Hutchins, M.U.3    Stevens, T.H.4    Klionsky, D.J.5
  • 60
    • 0037936890 scopus 로고    scopus 로고
    • From lysosomes to the plasma membrane: localization of vacuolar-type H+ -ATPase with the a3 isoform during osteoclast differentiation
    • Toyomura, T., Murata, Y., Yamamoto, A., Oka, T., Sun-Wada, G. H., Wada, Y. and Futai, M. (2003). From lysosomes to the plasma membrane: localization of vacuolar-type H+ -ATPase with the a3 isoform during osteoclast differentiation. J. Biol. Chem. 278, 22023-22030.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22023-22030
    • Toyomura, T.1    Murata, Y.2    Yamamoto, A.3    Oka, T.4    Sun-Wada, G.H.5    Wada, Y.6    Futai, M.7


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