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Volumn 107, Issue 29, 2010, Pages 12860-12865

Structural basis for the wobbler mouse neurodegenerative disorder caused by mutation in the Vps54 subunit of the GARP complex

Author keywords

Golgi apparatus; Protein stability; Vesicle trafficking; X ray crystallography

Indexed keywords

CELL MEMBRANE PROTEIN; CELL MEMBRANE PROTEIN GARP; LEUCINE; MEMBRANE PROTEIN; MEMBRANE PROTEIN VPS54; UNCLASSIFIED DRUG;

EID: 77955594318     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1004756107     Document Type: Article
Times cited : (62)

References (41)
  • 1
    • 34247623568 scopus 로고    scopus 로고
    • Coats, Tethers, Rabs, and SNAREs Work Together to Mediate the Intracellular Destination of a Transport Vesicle
    • DOI 10.1016/j.devcel.2007.04.005, PII S1534580707001529
    • Cai H, Reinisch K, Ferro-Novick S (2007) Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle. Dev Cell 12(5):671-682. (Pubitemid 46667749)
    • (2007) Developmental Cell , vol.12 , Issue.5 , pp. 671-682
    • Cai, H.1    Reinisch, K.2    Ferro-Novick, S.3
  • 2
    • 0033130103 scopus 로고    scopus 로고
    • Transport-vesicle targeting: Tethers before SNAREs
    • Pfeffer SR (1999) Transport-vesicle targeting: Tethers before SNAREs. Nat Cell Biol 1(1):E17-22.
    • (1999) Nat Cell Biol , vol.1 , Issue.1
    • Pfeffer, S.R.1
  • 3
    • 20544445438 scopus 로고    scopus 로고
    • Golgi tethering factors
    • Lupashin V, Sztul E (2005) Golgi tethering factors. Biochim Biophys Acta 1744(3):325-339.
    • (2005) Biochim Biophys Acta , vol.1744 , Issue.3 , pp. 325-339
    • Lupashin, V.1    Sztul, E.2
  • 4
    • 33644816187 scopus 로고    scopus 로고
    • Role of tethering factors in secretory membrane traffic
    • Sztul E, Lupashin V (2006) Role of tethering factors in secretory membrane traffic. Am J Physiol - Cell Physiol 290(1):C11-26.
    • (2006) Am J Physiol - Cell Physiol , vol.290 , Issue.1
    • Sztul, E.1    Lupashin, V.2
  • 5
    • 33745841364 scopus 로고    scopus 로고
    • The exocyst defrocked, a framework of rods revealed
    • DOI 10.1038/nsmb1097, PII NSMB1097
    • Munson M, Novick P (2006) The exocyst defrocked, a framework of rods revealed. Nat Struct Mol Biol 13(7):577-581. (Pubitemid 44036466)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.7 , pp. 577-581
    • Munson, M.1    Novick, P.2
  • 6
    • 67949091245 scopus 로고    scopus 로고
    • Vps-C complexes: Gatekeepers of endolysosomal traffic
    • Nickerson DP, Brett CL, Merz AJ (2009) Vps-C complexes: Gatekeepers of endolysosomal traffic. Curr Opin Cell Biol 21(4):543-551.
    • (2009) Curr Opin Cell Biol , vol.21 , Issue.4 , pp. 543-551
    • Nickerson, D.P.1    Brett, C.L.2    Merz, A.J.3
  • 7
    • 70450223107 scopus 로고    scopus 로고
    • Role of vesicle tethering factors in the ER-Golgi membrane traffic
    • Sztul E, Lupashin V (2009) Role of vesicle tethering factors in the ER-Golgi membrane traffic. FEBS Lett 583(23):3770-3783.
    • (2009) FEBS Lett , vol.583 , Issue.23 , pp. 3770-3783
    • Sztul, E.1    Lupashin, V.2
  • 8
    • 0035489304 scopus 로고    scopus 로고
    • The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic
    • Whyte JR, Munro S (2001) The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic. Dev Cell 1(4):527-537.
    • (2001) Dev Cell , vol.1 , Issue.4 , pp. 527-537
    • Whyte, J.R.1    Munro, S.2
  • 9
    • 33847648364 scopus 로고    scopus 로고
    • Control systems for membrane fusion in the ancestral eukaryote; evolution of tethering complexes and SM proteins
    • Koumandou VL, Dacks JB, Coulson RM, Field MC (2007) Control systems for membrane fusion in the ancestral eukaryote; evolution of tethering complexes and SM proteins. BMC Evol Biol 7:29.
    • (2007) BMC Evol Biol , vol.7 , pp. 29
    • Koumandou, V.L.1    Dacks, J.B.2    Coulson, R.M.3    Field, M.C.4
  • 10
    • 67651160303 scopus 로고    scopus 로고
    • Remote homology between Munc13 MUN domain and vesicle tethering complexes
    • Pei J, Ma C, Rizo J, Grishin NV (2009) Remote homology between Munc13 MUN domain and vesicle tethering complexes. J Mol Biol 391(3):509-517.
    • (2009) J Mol Biol , vol.391 , Issue.3 , pp. 509-517
    • Pei, J.1    Ma, C.2    Rizo, J.3    Grishin, N.V.4
  • 11
    • 28544432477 scopus 로고    scopus 로고
    • The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif
    • DOI 10.1038/nsmb1017
    • Dong G, Hutagalung AH, Fu C, Novick P, Reinisch KM (2005) The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif. Nat Struct Mol Biol 12(12):1094-1100. (Pubitemid 41746780)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.12 , pp. 1094-1100
    • Dong, G.1    Hutagalung, A.H.2    Fu, C.3    Novick, P.4    Reinisch, K.M.5
  • 12
    • 71149117138 scopus 로고    scopus 로고
    • A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1
    • Ren Y, et al. (2009) A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1. Cell 139(6):1119-1129.
    • (2009) Cell , vol.139 , Issue.6 , pp. 1119-1129
    • Ren, Y.1
  • 13
    • 59649120867 scopus 로고    scopus 로고
    • Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex
    • Tripathi A, Ren Y, Jeffrey PD, Hughson FM (2009) Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex. Nat Struct Mol Biol 16(2):114-123.
    • (2009) Nat Struct Mol Biol , vol.16 , Issue.2 , pp. 114-123
    • Tripathi, A.1    Ren, Y.2    Jeffrey, P.D.3    Hughson, F.M.4
  • 14
    • 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 (2000) Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late Golgi. Mol Biol Cell 11(1): 305-323.
    • (2000) Mol Biol Cell , vol.11 , Issue.1 , pp. 305-323
    • Conibear, E.1    Stevens, T.H.2
  • 15
    • 0037073694 scopus 로고    scopus 로고
    • Vps51p links the VFT complex to the SNARE Tlg1p
    • Siniossoglou S, Pelham HR (2002) Vps51p links the VFT complex to the SNARE Tlg1p. J Biol Chem 277(50):48318-48324.
    • (2002) J Biol Chem , vol.277 , Issue.50 , pp. 48318-48324
    • Siniossoglou, S.1    Pelham, H.R.2
  • 16
    • 0013468039 scopus 로고    scopus 로고
    • Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p
    • DOI 10.1091/mbc.E02-10-0654
    • Conibear E, Cleck JN, Stevens TH (2003) Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p. Mol Biol Cell 14(4):1610-1623. (Pubitemid 36547426)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.4 , pp. 1610-1623
    • Conibear, E.1    Cleck, J.N.2    Stevens, T.H.3
  • 17
    • 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 (2003) 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 278(7):5009-5020.
    • (2003) J Biol Chem , vol.278 , Issue.7 , pp. 5009-5020
    • Reggiori, F.1    Wang, C.W.2    Stromhaug, P.E.3    Shintani, T.4    Klionsky, D.J.5
  • 18
    • 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 (2008) Requirement of the human GARP complex for mannose 6-phosphate-receptor-dependent sorting of cathepsin D to lysosomes. Mol Biol Cell 19(6):2350-2362.
    • (2008) Mol Biol Cell , vol.19 , Issue.6 , pp. 2350-2362
    • Perez-Victoria, F.J.1    Mardones, G.A.2    Bonifacino, J.S.3
  • 20
    • 0642308225 scopus 로고    scopus 로고
    • The wobbler mouse: A neurodegeneration jigsaw puzzle
    • Boillee S, Peschanski M, Junier MP (2003) The wobbler mouse: A neurodegeneration jigsaw puzzle. Mol Neurobiol 28(1):65-106.
    • (2003) Mol Neurobiol , vol.28 , Issue.1 , pp. 65-106
    • Boillee, S.1    Peschanski, M.2    Junier, M.P.3
  • 21
    • 47249131665 scopus 로고    scopus 로고
    • Evaluation of the Golgi trafficking protein VPS54 (wobbler) as a candidate for ALS
    • Meisler MH, et al. (2008) Evaluation of the Golgi trafficking protein VPS54 (wobbler) as a candidate for ALS. Amyotroph Lateral Sc 9(3):141-148.
    • (2008) Amyotroph Lateral Sc , vol.9 , Issue.3 , pp. 141-148
    • Meisler, M.H.1
  • 22
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • DOI 10.1093/bioinformatics/btn507
    • Holm L, Kaariainen S, Rosenstrom P, Schenkel A (2008) Searching protein structure databases with DaliLite v.3.. Bioinformatics 24(23):2780-2781. (Pubitemid 352722625)
    • (2008) Bioinformatics , vol.24 , Issue.23 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 23
    • 33744933711 scopus 로고    scopus 로고
    • The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles
    • Sivaram MV, Furgason ML, Brewer DN, Munson M (2006) The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles. Nat Struct Mol Biol 13(6):555-556.
    • (2006) Nat Struct Mol Biol , vol.13 , Issue.6 , pp. 555-556
    • Sivaram, M.V.1    Furgason, M.L.2    Brewer, D.N.3    Munson, M.4
  • 24
    • 27144456598 scopus 로고    scopus 로고
    • Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo
    • DOI 10.1038/nsmb987, PII N987
    • Wu S, Mehta SQ, Pichaud F, Bellen HJ, Quiocho FA (2005) Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo. Nat Struct Mol Biol 12(10):879-885. (Pubitemid 41486711)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.10 , pp. 879-885
    • Wu, S.1    Mehta, S.Q.2    Pichaud, F.3    Bellen, H.J.4    Quiocho, F.A.5
  • 25
    • 34447276935 scopus 로고    scopus 로고
    • The crystal structure of mouse Exo70 reveals unique features of the mammalian exocyst
    • Moore BA, Robinson HH, Xu Z (2007) The crystal structure of mouse Exo70 reveals unique features of the mammalian exocyst. J Mol Biol 371(2):410-421.
    • (2007) J Mol Biol , vol.371 , Issue.2 , pp. 410-421
    • Moore, B.A.1    Robinson, H.H.2    Xu, Z.3
  • 26
    • 34548169619 scopus 로고    scopus 로고
    • Structural analysis of conserved oligomeric Golgi complex subunit 2
    • Cavanaugh LF, et al. (2007) Structural analysis of conserved oligomeric Golgi complex subunit 2. J Biol Chem 282(32):23418-23426.
    • (2007) J Biol Chem , vol.282 , Issue.32 , pp. 23418-23426
    • Cavanaugh, L.F.1
  • 27
    • 69449100200 scopus 로고    scopus 로고
    • Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene
    • Richardson BC, et al. (2009) Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene. Proc Natl Acad Sci USA 106(32):13329-13334.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.32 , pp. 13329-13334
    • Richardson, B.C.1
  • 28
    • 0033555677 scopus 로고    scopus 로고
    • A correlation between the loss of hydrophobic core packing interactions and protein stability
    • DOI 10.1006/jmbi.1998.2342
    • Vlassi M, Cesareni G, Kokkinidis M (1999) A correlation between the loss of hydrophobic core packing interactions and protein stability. J Mol Biol 285(2):817-827. (Pubitemid 29041810)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.2 , pp. 817-827
    • Vlassi, M.1    Cesareni, G.2    Kokkinidis, M.3
  • 29
    • 75649097134 scopus 로고    scopus 로고
    • Intrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: Comparison with other hydrophilicity/hydrophobicity scales
    • Mant CT, Kovacs JM, Kim HM, Pollock DD, Hodges RS (2009) Intrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: Comparison with other hydrophilicity/hydrophobicity scales. Biopolymers 92(6):573-595.
    • (2009) Biopolymers , vol.92 , Issue.6 , pp. 573-595
    • Mant, C.T.1    Kovacs, J.M.2    Kim, H.M.3    Pollock, D.D.4    Hodges, R.S.5
  • 30
    • 33745366486 scopus 로고    scopus 로고
    • Domains within the GARP subunit Vps54 confer separate functions in complex assembly and early endosome recognition
    • Quenneville NR, Chao TY, McCaffery JM, Conibear E (2006) Domains within the GARP subunit Vps54 confer separate functions in complex assembly and early endosome recognition. Mol Biol Cell 17(4):1859-1870.
    • (2006) Mol Biol Cell , vol.17 , Issue.4 , pp. 1859-1870
    • Quenneville, N.R.1    Chao, T.Y.2    McCaffery, J.M.3    Conibear, E.4
  • 31
    • 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 (2009) Dual roles of the mammalian GARP complex in tethering and SNARE complex assembly at the trans-Golgi network. Mol Cell Biol 29(19):5251-5263.
    • (2009) Mol Cell Biol , vol.29 , Issue.19 , pp. 5251-5263
    • Perez-Victoria, F.J.1    Bonifacino, J.S.2
  • 33
    • 0034666116 scopus 로고    scopus 로고
    • Cathepsin D deficiency induces lysosomal storage with ceroid lipofuscin in mouse CNS neurons
    • Koike M, et al. (2000) Cathepsin D deficiency induces lysosomal storage with ceroid lipofuscin in mouse CNS neurons. J Neurosci 20(18):6898-6906.
    • (2000) J Neurosci , vol.20 , Issue.18 , pp. 6898-6906
    • Koike, M.1
  • 35
    • 0031080386 scopus 로고    scopus 로고
    • TRPM-2 expression and TUNEL staining in neurodegenerative diseases: Studies in wobbler and rd mice
    • DOI 10.1006/exnr.1996.6364
    • Popper P, Farber DB, Micevych PE, Minoofar K, Bronstein JM (1997) TRPM-2 expression and tunel staining in neurodegenerative diseases: Studies in wobbler and rd mice. Exp Neurol 143(2):246-254. (Pubitemid 27148229)
    • (1997) Experimental Neurology , vol.143 , Issue.2 , pp. 246-254
    • Popper, P.1    Farber, D.B.2    Micevych, P.E.3    Minoofar, K.4    Bronstein, J.M.5
  • 36
    • 0345578686 scopus 로고    scopus 로고
    • Progesterone neuroprotection in the Wobbler mouse, a genetic model of spinal cord motor neuron disease
    • Gonzalez Deniselle MC, et al. (2002) Progesterone neuroprotection in the Wobbler mouse, a genetic model of spinal cord motor neuron disease. Neurobiol Dis 11(3): 457-468.
    • (2002) Neurobiol Dis , vol.11 , Issue.3 , pp. 457-468
    • Gonzalez Deniselle, M.C.1
  • 39
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Anonymous
    • Anonymous (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D 50(Pt 5):760-763.
    • (1994) Acta Crystallogr D , vol.50 , Issue.PART 5 , pp. 760-763
  • 40
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D 60(Pt 12, Pt 1):2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , Issue.PART 12 AND PART 1 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 41
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D 66(Pt 2):213-221.
    • Acta Crystallogr D , vol.66 , Issue.PART 2 , pp. 213-221
    • Adams, P.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.