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Volumn 11, Issue 5, 2010, Pages 688-705

A Novel Syntaxin 6-Interacting protein, SHIP164, regulates Syntaxin 6-Dependent sorting from early endosomes

Author keywords

GARP; Intracellular transport; KIAA0701; SNAREs; Trans Golgi network; UHRF1BP1L; VFT; Vps13

Indexed keywords

CATION; CELL PROTEIN; GOLGI ASSOCIATED RETROGRADE PROTEIN; PROTEIN SHIP164; REGULATOR PROTEIN; SOMATOMEDIN B RECEPTOR; SYNTAXIN; SYNTAXIN 6; TRANSFERRIN RECEPTOR; UNCLASSIFIED DRUG;

EID: 77953141420     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2010.01049.x     Document Type: Article
Times cited : (28)

References (45)
  • 2
    • 33845991859 scopus 로고    scopus 로고
    • SNARE status regulates tether recruitment and function in homotypic COPII vesicle fusion
    • Bentley M, Liang Y, Mullen K, Xu D, Sztul E, Hay JC. SNARE status regulates tether recruitment and function in homotypic COPII vesicle fusion. J Biol Chem 2006, 281:38825-38833.
    • (2006) J Biol Chem , vol.281 , pp. 38825-38833
    • Bentley, M.1    Liang, Y.2    Mullen, K.3    Xu, D.4    Sztul, E.5    Hay, J.C.6
  • 3
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer D, Sutton RB, Brunger AT, Jahn R. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc Natl Acad Sci U S A 1998, 95:15781-15786.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 4
    • 35748984692 scopus 로고    scopus 로고
    • Munc18-1 in secretion: lonely Munc joins SNARE team and takes control
    • Toonen RF, Verhage M. Munc18-1 in secretion: lonely Munc joins SNARE team and takes control. Trends Neurosci 2007, 30:564-572.
    • (2007) Trends Neurosci , vol.30 , pp. 564-572
    • Toonen, R.F.1    Verhage, M.2
  • 5
    • 36049049393 scopus 로고    scopus 로고
    • Dual modes of Munc18-1/SNARE interactions are coupled by functionally critical binding to syntaxin-1 N terminus
    • Khvotchev M, Dulubova I, Sun J, Dai H, Rizo J, Sudhof TC. Dual modes of Munc18-1/SNARE interactions are coupled by functionally critical binding to syntaxin-1 N terminus. J Neurosci 2007, 27:12147-12155.
    • (2007) J Neurosci , vol.27 , pp. 12147-12155
    • Khvotchev, M.1    Dulubova, I.2    Sun, J.3    Dai, H.4    Rizo, J.5    Sudhof, T.C.6
  • 6
    • 33745241903 scopus 로고    scopus 로고
    • The Sec1p /Munc18 protein Vps45p binds its cognate SNARE proteins via two distinct modes
    • Carpp LN, Ciufo LF, Shanks SG, Boyd A, Bryant NJ. The Sec1p /Munc18 protein Vps45p binds its cognate SNARE proteins via two distinct modes. J Cell Biol 2006, 173:927-936.
    • (2006) J Cell Biol , vol.173 , pp. 927-936
    • Carpp, L.N.1    Ciufo, L.F.2    Shanks, S.G.3    Boyd, A.4    Bryant, N.J.5
  • 8
    • 36549042931 scopus 로고    scopus 로고
    • A SNARE-adaptor interaction is a new mode of cargo recognition in clathrin-coated vesicles
    • Miller SE, Collins BM, McCoy AJ, Robinson MS, Owen DJ. A SNARE-adaptor interaction is a new mode of cargo recognition in clathrin-coated vesicles. Nature 2007, 450:570-574.
    • (2007) Nature , vol.450 , pp. 570-574
    • Miller, S.E.1    Collins, B.M.2    McCoy, A.J.3    Robinson, M.S.4    Owen, D.J.5
  • 9
    • 0037073694 scopus 로고    scopus 로고
    • Vps51p links the VFT complex to the SNARE Tlg1p
    • Siniossoglou S, Pelham HR. Vps51p links the VFT complex to the SNARE Tlg1p. J Biol Chem 2002, 277:48318-48324.
    • (2002) J Biol Chem , vol.277 , pp. 48318-48324
    • Siniossoglou, S.1    Pelham, H.R.2
  • 10
    • 0037737745 scopus 로고    scopus 로고
    • Vps51 is part of the yeast Vps fifty-three tethering complex essential for retrograde traffic from the early endosome and Cvt vesicle completion
    • Reggiori F, Wang CW, Stromhaug PE, Shintani T, Klionsky DJ. Vps51 is part of the yeast Vps fifty-three tethering complex essential for retrograde traffic from the early endosome and Cvt vesicle completion. J Biol Chem 2003, 278:5009-5020.
    • (2003) J Biol Chem , vol.278 , pp. 5009-5020
    • Reggiori, F.1    Wang, C.W.2    Stromhaug, P.E.3    Shintani, T.4    Klionsky, D.J.5
  • 11
    • 0013468039 scopus 로고    scopus 로고
    • Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p
    • Conibear E, Cleck JN, Stevens TH. Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p. Mol Biol Cell 2003, 14:1610-1623.
    • (2003) Mol Biol Cell , vol.14 , pp. 1610-1623
    • Conibear, E.1    Cleck, J.N.2    Stevens, T.H.3
  • 12
    • 0032879685 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 interacts directly with syntaxin-6
    • Simonsen A, Gaullier JM, D'Arrigo A, Stenmark H. The Rab5 effector EEA1 interacts directly with syntaxin-6. J Biol Chem 1999, 274:28857-28860.
    • (1999) J Biol Chem , vol.274 , pp. 28857-28860
    • Simonsen, A.1    Gaullier, J.M.2    D'Arrigo, A.3    Stenmark, H.4
  • 13
    • 16344381891 scopus 로고    scopus 로고
    • MARCH-II is a syntaxin-6-binding protein involved in endosomal trafficking
    • Nakamura N, Fukuda H, Kato A, Hirose S. MARCH-II is a syntaxin-6-binding protein involved in endosomal trafficking. Mol Biol Cell 2005, 16:1696-1710.
    • (2005) Mol Biol Cell , vol.16 , pp. 1696-1710
    • Nakamura, N.1    Fukuda, H.2    Kato, A.3    Hirose, S.4
  • 14
    • 32944455458 scopus 로고    scopus 로고
    • MARCH-III is a novel component of endosomes with properties similar to those of MARCH-II
    • Fukuda H, Nakamura N, Hirose S. MARCH-III is a novel component of endosomes with properties similar to those of MARCH-II. J Biochem (Tokyo) 2006, 139:137-145.
    • (2006) J Biochem (Tokyo) , vol.139 , pp. 137-145
    • Fukuda, H.1    Nakamura, N.2    Hirose, S.3
  • 15
    • 0034812092 scopus 로고    scopus 로고
    • Identification of a PDZ domain containing Golgi protein, GOPC, as an interaction partner of frizzled
    • Yao R, Maeda T, Takada S, Noda T. Identification of a PDZ domain containing Golgi protein, GOPC, as an interaction partner of frizzled. Biochem Biophys Res Commun 2001, 286:771-778.
    • (2001) Biochem Biophys Res Commun , vol.286 , pp. 771-778
    • Yao, R.1    Maeda, T.2    Takada, S.3    Noda, T.4
  • 16
    • 0034806856 scopus 로고    scopus 로고
    • PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10
    • Neudauer CL, Joberty G, Macara IG. PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10. Biochem Biophys Res Commun 2001, 280:541-547.
    • (2001) Biochem Biophys Res Commun , vol.280 , pp. 541-547
    • Neudauer, C.L.1    Joberty, G.2    Macara, I.G.3
  • 18
    • 0035800743 scopus 로고    scopus 로고
    • Association of a novel PDZ domain-containing peripheral Golgi protein with the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor) protein syntaxin 6
    • Charest A, Lane K, McMahon K, Housman DE. Association of a novel PDZ domain-containing peripheral Golgi protein with the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor) protein syntaxin 6. J Biol Chem 2001, 276:29456-29465.
    • (2001) J Biol Chem , vol.276 , pp. 29456-29465
    • Charest, A.1    Lane, K.2    McMahon, K.3    Housman, D.E.4
  • 19
    • 70349319578 scopus 로고    scopus 로고
    • Dual roles of the mammalian GARP complex in tethering and SNARE complex assembly at the trans-golgi network
    • Perez-Victoria FJ, Bonifacino JS. Dual roles of the mammalian GARP complex in tethering and SNARE complex assembly at the trans-golgi network. Mol Cell Biol 2009, 29:5251-5263.
    • (2009) Mol Cell Biol , vol.29 , pp. 5251-5263
    • Perez-Victoria, F.J.1    Bonifacino, J.S.2
  • 20
    • 0035158011 scopus 로고    scopus 로고
    • Homotypic fusion of immature secretory granules during maturation requires syntaxin 6
    • Wendler F, Page L, Urbe S, Tooze SA. Homotypic fusion of immature secretory granules during maturation requires syntaxin 6. Mol Biol Cell 2001, 12:1699-1709.
    • (2001) Mol Biol Cell , vol.12 , pp. 1699-1709
    • Wendler, F.1    Page, L.2    Urbe, S.3    Tooze, S.A.4
  • 21
    • 43049130794 scopus 로고    scopus 로고
    • Syntaxin 6 regulates nerve growth factor-dependent neurite outgrowth
    • Kabayama H, Tokushige N, Takeuchi M, Mikoshiba K. Syntaxin 6 regulates nerve growth factor-dependent neurite outgrowth. Neurosci Lett 2008, 436:340-344.
    • (2008) Neurosci Lett , vol.436 , pp. 340-344
    • Kabayama, H.1    Tokushige, N.2    Takeuchi, M.3    Mikoshiba, K.4
  • 22
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2006, 127:635-648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 23
    • 0032580809 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro.
    • Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O. Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res 1998, 5:169-176.
    • (1998) DNA Res , vol.5 , pp. 169-176
    • Ishikawa, K.1    Nagase, T.2    Suyama, M.3    Miyajima, N.4    Tanaka, A.5    Kotani, H.6    Nomura, N.7    Ohara, O.8
  • 24
    • 0031588576 scopus 로고    scopus 로고
    • Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins
    • Ohara O, Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Nomura N. Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins. DNA Res 1997, 4:53-59.
    • (1997) DNA Res , vol.4 , pp. 53-59
    • Ohara, O.1    Nagase, T.2    Ishikawa, K.3    Nakajima, D.4    Ohira, M.5    Seki, N.6    Nomura, N.7
  • 25
    • 0030762073 scopus 로고    scopus 로고
    • SOI1 encodes a novel, conserved protein that promotes TGN-endosomal cycling of Kex2p and other membrane proteins by modulating the function of two TGN localization signals
    • Brickner JH, Fuller RS. SOI1 encodes a novel, conserved protein that promotes TGN-endosomal cycling of Kex2p and other membrane proteins by modulating the function of two TGN localization signals. J Cell Biol 1997, 139:23-36.
    • (1997) J Cell Biol , vol.139 , pp. 23-36
    • Brickner, J.H.1    Fuller, R.S.2
  • 26
    • 0029833575 scopus 로고    scopus 로고
    • Allele-specific suppression of a defective trans-Golgi network (TGN) localization signal in Kex2p identifies three genes involved in localization of TGN transmembrane proteins
    • Redding K, Brickner JH, Marschall LG, Nichols JW, Fuller RS. Allele-specific suppression of a defective trans-Golgi network (TGN) localization signal in Kex2p identifies three genes involved in localization of TGN transmembrane proteins. Mol Cell Biol 1996, 16:6208-6217.
    • (1996) Mol Cell Biol , vol.16 , pp. 6208-6217
    • Redding, K.1    Brickner, J.H.2    Marschall, L.G.3    Nichols, J.W.4    Fuller, R.S.5
  • 28
    • 7044245474 scopus 로고    scopus 로고
    • ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain
    • Unoki M, Nishidate T, Nakamura Y. ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain. Oncogene 2004, 23:7601-7610.
    • (2004) Oncogene , vol.23 , pp. 7601-7610
    • Unoki, M.1    Nishidate, T.2    Nakamura, Y.3
  • 29
    • 0033105847 scopus 로고    scopus 로고
    • The endosome fusion regulator early-endosomal autoantigen 1 (EEA1) is a dimer
    • Callaghan J, Simonsen A, Gaullier JM, Toh BH, Stenmark H. The endosome fusion regulator early-endosomal autoantigen 1 (EEA1) is a dimer. Biochem J 1999, 338:539-543.
    • (1999) Biochem J , vol.338 , pp. 539-543
    • Callaghan, J.1    Simonsen, A.2    Gaullier, J.M.3    Toh, B.H.4    Stenmark, H.5
  • 30
    • 21744438286 scopus 로고    scopus 로고
    • The trans-Golgi network GRIP-domain proteins form alpha-helical homodimers
    • Luke MR, Houghton F, Perugini MA, Gleeson PA. The trans-Golgi network GRIP-domain proteins form alpha-helical homodimers. Biochem J 2005, 388:835-841.
    • (2005) Biochem J , vol.388 , pp. 835-841
    • Luke, M.R.1    Houghton, F.2    Perugini, M.A.3    Gleeson, P.A.4
  • 31
    • 0030797279 scopus 로고    scopus 로고
    • Syntaxin 6 functions in trans-Golgi network vesicle trafficking
    • Bock JB, Klumperman J, Davanger S, Scheller RH. Syntaxin 6 functions in trans-Golgi network vesicle trafficking. Mol Biol Cell 1997, 8:1261-1271.
    • (1997) Mol Biol Cell , vol.8 , pp. 1261-1271
    • Bock, J.B.1    Klumperman, J.2    Davanger, S.3    Scheller, R.H.4
  • 33
    • 0035503740 scopus 로고    scopus 로고
    • An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes
    • Siniossoglou S, Pelham HR. An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes. EMBO J 2001, 20:5991-5998.
    • (2001) EMBO J , vol.20 , pp. 5991-5998
    • Siniossoglou, S.1    Pelham, H.R.2
  • 34
    • 0037418595 scopus 로고    scopus 로고
    • The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts with vesicle-tethering factors at the Golgi apparatus
    • Panic B, Whyte JR, Munro S. The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts with vesicle-tethering factors at the Golgi apparatus. Curr Biol 2003, 13:405-410.
    • (2003) Curr Biol , vol.13 , pp. 405-410
    • Panic, B.1    Whyte, J.R.2    Munro, S.3
  • 35
    • 48749111661 scopus 로고    scopus 로고
    • Requirement of the human GARP complex for mannose 6-phosphate-receptor-dependent sorting of cathepsin D to lysosomes
    • Perez-Victoria FJ, Mardones GA, Bonifacino JS. Requirement of the human GARP complex for mannose 6-phosphate-receptor-dependent sorting of cathepsin D to lysosomes. Mol Biol Cell 2008, 19:2350-2362.
    • (2008) Mol Biol Cell , vol.19 , pp. 2350-2362
    • Perez-Victoria, F.J.1    Mardones, G.A.2    Bonifacino, J.S.3
  • 37
    • 33746092492 scopus 로고    scopus 로고
    • Flat clathrin coats on endosomes mediate degradative protein sorting by scaffolding Hrs in dynamic microdomains
    • Raiborg C, Wesche J, Malerod L, Stenmark H. Flat clathrin coats on endosomes mediate degradative protein sorting by scaffolding Hrs in dynamic microdomains. J Cell Sci 2006, 119:2414-2424.
    • (2006) J Cell Sci , vol.119 , pp. 2414-2424
    • Raiborg, C.1    Wesche, J.2    Malerod, L.3    Stenmark, H.4
  • 38
    • 0033972955 scopus 로고    scopus 로고
    • Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late Golgi
    • Conibear E, Stevens TH. Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late Golgi. Mol Biol Cell 2000, 11:305-323.
    • (2000) Mol Biol Cell , vol.11 , pp. 305-323
    • Conibear, E.1    Stevens, T.H.2
  • 39
    • 37049000164 scopus 로고    scopus 로고
    • The golgin GCC88 is required for efficient retrograde transport of cargo from the early endosomes to the trans-Golgi network
    • Lieu ZZ, Derby MC, Teasdale RD, Hart C, Gunn P, Gleeson PA. The golgin GCC88 is required for efficient retrograde transport of cargo from the early endosomes to the trans-Golgi network. Mol Biol Cell 2007, 18:4979-4991.
    • (2007) Mol Biol Cell , vol.18 , pp. 4979-4991
    • Lieu, Z.Z.1    Derby, M.C.2    Teasdale, R.D.3    Hart, C.4    Gunn, P.5    Gleeson, P.A.6
  • 40
    • 38349014268 scopus 로고    scopus 로고
    • A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells
    • Ganley IG, Espinosa E, Pfeffer SR. A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells. J Cell Biol 2008, 180:159-172.
    • (2008) J Cell Biol , vol.180 , pp. 159-172
    • Ganley, I.G.1    Espinosa, E.2    Pfeffer, S.R.3
  • 43
    • 0034280113 scopus 로고    scopus 로고
    • Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing
    • Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S. Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. EMBO Rep 2000, 1:287-292.
    • (2000) EMBO Rep , vol.1 , pp. 287-292
    • Simpson, J.C.1    Wellenreuther, R.2    Poustka, A.3    Pepperkok, R.4    Wiemann, S.5


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