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Volumn 4, Issue 2, 2013, Pages 62-69

Discovery of new longin and roadblock domains that form platforms for small GTPases in ragulator and TRAPP-II

Author keywords

C7orf59; C9orf72; DENNL72; HBXIP; HHpred; NPRL2; NPRL3; Trs130p; YCR075W A; YNR034W A

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 1; CELL PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; HBXIP PROTEIN; PROTEIN C7ORF59; RAB11 PROTEIN; SNARE PROTEIN; TORC1 PROTEIN; TRANSPORT PROTEIN PARTICLE C1 PROTEIN; TRANSPORT PROTEIN PARTICLE C10 PROTEIN; TRANSPORT PROTEIN PARTICLE II; UNCLASSIFIED DRUG;

EID: 84876431000     PISSN: 21541248     EISSN: 21541256     Source Type: Journal    
DOI: 10.4161/sgtp.24262     Document Type: Article
Times cited : (75)

References (54)
  • 1
    • 77958471298 scopus 로고    scopus 로고
    • Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors
    • PMID:20937701; DOI:10.1083/jcb.201008051
    • YoshimuraS, GerondopoulosA, LinfordA, RigdenDJ, BarrFA. Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors. J Cell Biol2010; 191:367-381; PMID:20937701; DOI:10.1083/jcb.201008051.
    • (2010) J Cell Biol , vol.191 , pp. 367-381
    • Yoshimura, S.1    Gerondopoulos, A.2    Linford, A.3    Rigden, D.J.4    Barr, F.A.5
  • 2
    • 84869491973 scopus 로고    scopus 로고
    • BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine nucleotide exchange factor
    • PMID:23084991; DOI:10.1016/j.cub.2012.09.020
    • GerondopoulosA, LangemeyerL, LiangJR, LinfordA, BarrFA. BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine nucleotide exchange factor. Curr Biol2012; 22:2135-2139; PMID:23084991; DOI:10.1016/j.cub.2012.09.020.
    • (2012) Curr Biol , vol.22 , pp. 2135-2139
    • Gerondopoulos, A.1    Langemeyer, L.2    Liang, J.R.3    Linford, A.4    Barr, F.A.5
  • 3
    • 84865378898 scopus 로고    scopus 로고
    • Untangling the evolution of Rab G proteins: Implications of a comprehensive genomic analysis
    • PMID:22873208; DOI:10.1186/1741-7007-10-71
    • KlöpperTH, KienleN, FasshauerD, MunroS. Untangling the evolution of Rab G proteins: implications of a comprehensive genomic analysis. BMC Biol2012; 10:71; PMID:22873208; DOI:10.1186/1741-7007-10-71.
    • (2012) BMC Biol , vol.10 , pp. 71
    • Klöpper, T.H.1    Kienle, N.2    Fasshauer, D.3    Munro, S.4
  • 4
    • 0041806509 scopus 로고    scopus 로고
    • A dual mechanism controlling the localization and function of exocytic v-SNAREs
    • PMID:12853575; DOI:10.1073/pnas.1431910100
    • Martinez-ArcaS, RudgeR, VaccaM, RaposoG, CamonisJ, Proux-GillardeauxV, et al. A dual mechanism controlling the localization and function of exocytic v-SNAREs. Proc Natl Acad Sci U S A2003; 100:9011-9016; PMID:12853575; DOI:10.1073/pnas.1431910100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 9011-9016
    • Martinez-Arca, S.1    Rudge, R.2    Vacca, M.3    Raposo, G.4    Camonis, J.5    Proux-Gillardeaux, V.6
  • 5
    • 84870799578 scopus 로고    scopus 로고
    • The binding of Varp to VAMP7 traps VAMP7 in a closed, fusogenically inactive conformation
    • PMID:23104059; DOI:10.1038/nsmb.2414
    • SchäferIB, HeskethGG, BrightNA, GraySR, PryorPR, EvansPR, et al. The binding of Varp to VAMP7 traps VAMP7 in a closed, fusogenically inactive conformation. Nat Struct Mol Biol2012; 19:1300-1309; PMID:23104059; DOI:10.1038/nsmb.2414.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 1300-1309
    • Schäfer, I.B.1    Hesketh, G.G.2    Bright, N.A.3    Gray, S.R.4    Pryor, P.R.5    Evans, P.R.6
  • 6
    • 34247380779 scopus 로고    scopus 로고
    • Multiple and stepwise interactions between coatomer and ADP-ribosylation factor-1 (Arf1)-GTP
    • PMID:17451557; DOI:10.1111/j.1600-0854.2007.00554.x
    • SunZ, AnderlF, FröhlichK, ZhaoL, HankeS, BrüggerB, et al. Multiple and stepwise interactions between coatomer and ADP-ribosylation factor-1 (Arf1)-GTP. Traffic2007; 8:582-593; PMID:17451557; DOI:10.1111/j.1600-0854.2007.00554.x.
    • (2007) Traffic , vol.8 , pp. 582-593
    • Sun, Z.1    Anderl, F.2    Fröhlich, K.3    Zhao, L.4    Hanke, S.5    Brügger, B.6
  • 8
    • 0035964822 scopus 로고    scopus 로고
    • uDENN, DENN, and dDENN: Indissociable domains in Rab and MAP kinases signaling pathways
    • PMID:11563850; DOI:10.1006/bbrc.2001.5652
    • LevivierE, GoudB, SouchetM, CalmelsTP, MornonJP, CallebautI. uDENN, DENN, and dDENN: indissociable domains in Rab and MAP kinases signaling pathways. Biochem Biophys Res Commun2001; 287:688-695; PMID:11563850; DOI:10.1006/bbrc.2001.5652.
    • (2001) Biochem Biophys Res Commun , vol.287 , pp. 688-695
    • Levivier, E.1    Goud, B.2    Souchet, M.3    Calmels, T.P.4    Mornon, J.P.5    Callebaut, I.6
  • 9
    • 3342936383 scopus 로고    scopus 로고
    • Crystal structure of the p14/MP1 scaffolding complex: How a twin couple attaches mitogen-activated protein kinase signaling to late endosomes
    • PMID:15263099; DOI:10.1073/pnas.0403435101
    • KurzbauerR, TeisD, de AraujoME, Maurer-StrohS, EisenhaberF, BourenkovGP, et al. Crystal structure of the p14/MP1 scaffolding complex: how a twin couple attaches mitogen-activated protein kinase signaling to late endosomes. Proc Natl Acad Sci U S A2004; 101:10984-10989; PMID:15263099; DOI:10.1073/pnas.0403435101.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10984-10989
    • Kurzbauer, R.1    Teis, D.2    de Araujo, M.E.3    Maurer-Stroh, S.4    Eisenhaber, F.5    Bourenkov, G.P.6
  • 10
    • 80054934194 scopus 로고    scopus 로고
    • Structural analysis of the Ras-like G protein MglA and its cognate GAP MglB and implications for bacterial polarity
    • PMID:21847100; DOI:10.1038/emboj.2011.291
    • MiertzschkeM, KoernerC, VetterIR, KeilbergD, HotE, LeonardyS, et al. Structural analysis of the Ras-like G protein MglA and its cognate GAP MglB and implications for bacterial polarity. EMBO J2011; 30:4185-4197; PMID:21847100; DOI:10.1038/emboj.2011.291.
    • (2011) EMBO J , vol.30 , pp. 4185-4197
    • Miertzschke, M.1    Koerner, C.2    Vetter, I.R.3    Keilberg, D.4    Hot, E.5    Leonardy, S.6
  • 11
    • 33646461205 scopus 로고    scopus 로고
    • The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domains
    • PMID:16439358; DOI:10.1074/jbc.M512415200
    • SchlenkerO, HendricksA, SinningI, WildK. The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domains. J Biol Chem2006; 281:8898-8906; PMID:16439358; DOI:10.1074/jbc.M512415200.
    • (2006) J Biol Chem , vol.281 , pp. 8898-8906
    • Schlenker, O.1    Hendricks, A.2    Sinning, I.3    Wild, K.4
  • 12
    • 45449083834 scopus 로고    scopus 로고
    • The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes
    • PMID:18585354; DOI:10.1016/j.cell.2008.04.049
    • CaiY, ChinHF, LazarovaD, MenonS, FuC, CaiH, et al. The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes. Cell2008; 133:1202-1213; PMID:18585354; DOI:10.1016/j.cell.2008.04.049.
    • (2008) Cell , vol.133 , pp. 1202-1213
    • Cai, Y.1    Chin, H.F.2    Lazarova, D.3    Menon, S.4    Fu, C.5    Cai, H.6
  • 13
    • 81755163615 scopus 로고    scopus 로고
    • Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate
    • PMID:22065758; DOI:10.1073/pnas.1110415108
    • WuX, BradleyMJ, CaiY, KümmelD, De La CruzEM, BarrFA, et al. Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate. Proc Natl Acad Sci U S A2011; 108:18672-18677; PMID:22065758; DOI:10.1073/pnas.1110415108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 18672-18677
    • Wu, X.1    Bradley, M.J.2    Cai, Y.3    Kümmel, D.4    De La Cruz, E.M.5    Barr, F.A.6
  • 14
    • 80051873144 scopus 로고    scopus 로고
    • Crystal structure of the Gtr1p-Gtr2p complex reveals new insights into the amino acid-induced TORC1 activation
    • PMID:21816923; DOI:10.1101/gad.16968011
    • GongR, LiL, LiuY, WangP, YangH, WangL, et al. Crystal structure of the Gtr1p-Gtr2p complex reveals new insights into the amino acid-induced TORC1 activation. Genes Dev2011; 25:1668-1673; PMID:21816923; DOI:10.1101/gad.16968011.
    • (2011) Genes Dev , vol.25 , pp. 1668-1673
    • Gong, R.1    Li, L.2    Liu, Y.3    Wang, P.4    Yang, H.5    Wang, L.6
  • 15
    • 84865492819 scopus 로고    scopus 로고
    • Crystal structure of the Gtr1p(GTP)-Gtr2p(GDP) protein complex reveals large structural rearrangements triggered by GTP-to-GDP conversion
    • PMID:22807443; DOI:10.1074/jbc.C112.384420
    • JeongJH, LeeKH, KimYM, KimDH, OhBH, KimYG. Crystal structure of the Gtr1p(GTP)-Gtr2p(GDP) protein complex reveals large structural rearrangements triggered by GTP-to-GDP conversion. J Biol Chem2012; 287:29648-29653; PMID:22807443; DOI:10.1074/jbc.C112.384420.
    • (2012) J Biol Chem , vol.287 , pp. 29648-29653
    • Jeong, J.H.1    Lee, K.H.2    Kim, Y.M.3    Kim, D.H.4    Oh, B.H.5    Kim, Y.G.6
  • 16
    • 84870530032 scopus 로고    scopus 로고
    • Ego3 functions as a homodimer to mediate the interaction between Gtr1-Gtr2 and Ego1 in the ego complex to activate TORC1
    • PMID:23123112; DOI:10.1016/j.str.2012.09.019
    • ZhangT, Péli-GulliMP, YangH, De VirgilioC, DingJ. Ego3 functions as a homodimer to mediate the interaction between Gtr1-Gtr2 and Ego1 in the ego complex to activate TORC1. Structure2012; 20:2151-2160; PMID:23123112; DOI:10.1016/j.str.2012.09.019.
    • (2012) Structure , vol.20 , pp. 2151-2160
    • Zhang, T.1    Péli-Gulli, M.P.2    Yang, H.3    de Virgilio, C.4    Ding, J.5
  • 17
    • 45849105156 scopus 로고    scopus 로고
    • The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1
    • PMID:18497260; DOI:10.1126/science.1157535
    • SancakY, PetersonTR, ShaulYD, LindquistRA, ThoreenCC, Bar-PeledL, et al. The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science2008; 320:1496-1501; PMID:18497260; DOI:10.1126/science.1157535.
    • (2008) Science , vol.320 , pp. 1496-1501
    • Sancak, Y.1    Peterson, T.R.2    Shaul, Y.D.3    Lindquist, R.A.4    Thoreen, C.C.5    Bar-Peled, L.6
  • 18
    • 79954614556 scopus 로고    scopus 로고
    • DENN domain proteins: Regulators of Rab GTPases
    • PMID:21330364; DOI:10.1074/jbc.R110.217067
    • MaratAL, DokainishH, McPhersonPS. DENN domain proteins: regulators of Rab GTPases. J Biol Chem2011; 286:13791-13800; PMID:21330364; DOI:10.1074/jbc.R110.217067.
    • (2011) J Biol Chem , vol.286 , pp. 13791-13800
    • Marat, A.L.1    Dokainish, H.2    McPherson, P.S.3
  • 19
    • 84870859143 scopus 로고    scopus 로고
    • Crystal structure of folliculin reveals a hidDENN function in genetically inherited renal cancer
    • PMID:22977732; DOI:10.1098/rsob.120071
    • NookalaRK, LangemeyerL, PacittoA, Ochoa-MontañoB, DonaldsonJC, BlaszczykBK, et al. Crystal structure of folliculin reveals a hidDENN function in genetically inherited renal cancer. Open Biol2012; 2:120071; PMID:22977732; DOI:10.1098/rsob.120071.
    • (2012) Open Biol , vol.2 , pp. 120071
    • Nookala, R.K.1    Langemeyer, L.2    Pacitto, A.3    Ochoa-Montaño, B.4    Donaldson, J.C.5    Blaszczyk, B.K.6
  • 20
    • 38449122032 scopus 로고    scopus 로고
    • Kidney-targeted Birt-Hogg-Dube gene inactivation in a mouse model: Erk1/2 and Akt-mTOR activation, cell hyperproliferation, and polycystic kidneys
    • PMID:18182616; DOI:10.1093/jnci/djm288
    • BabaM, FurihataM, HongSB, TessarolloL, HainesDC, SouthonE, et al. Kidney-targeted Birt-Hogg-Dube gene inactivation in a mouse model: Erk1/2 and Akt-mTOR activation, cell hyperproliferation, and polycystic kidneys. J Natl Cancer Inst2008; 100:140-154; PMID:18182616; DOI:10.1093/jnci/djm288.
    • (2008) J Natl Cancer Inst , vol.100 , pp. 140-154
    • Baba, M.1    Furihata, M.2    Hong, S.B.3    Tessarollo, L.4    Haines, D.C.5    Southon, E.6
  • 21
    • 77953801358 scopus 로고    scopus 로고
    • Regulation of mTORC1 by the Rab and Arf GTPases
    • PMID:20457610; DOI:10.1074/jbc.C110.102483
    • LiL, KimE, YuanH, InokiK, Goraksha-HicksP, SchiesherRL, et al. Regulation of mTORC1 by the Rab and Arf GTPases. J Biol Chem2010; 285:19705-19709; PMID:20457610; DOI:10.1074/jbc.C110.102483.
    • (2010) J Biol Chem , vol.285 , pp. 19705-19709
    • Li, L.1    Kim, E.2    Yuan, H.3    Inoki, K.4    Goraksha-Hicks, P.5    Schiesher, R.L.6
  • 22
    • 47749102551 scopus 로고    scopus 로고
    • Afi1p functions as an Arf3p polarization-specific docking factor for development of polarity
    • PMID:18397879; DOI:10.1074/jbc.M802550200
    • TsaiPC, LeeSW, LiuYW, ChuCW, ChenKY, HoJC, et al. Afi1p functions as an Arf3p polarization-specific docking factor for development of polarity. J Biol Chem2008; 283:16915-16927; PMID:18397879; DOI:10.1074/jbc.M802550200.
    • (2008) J Biol Chem , vol.283 , pp. 16915-16927
    • Tsai, P.C.1    Lee, S.W.2    Liu, Y.W.3    Chu, C.W.4    Chen, K.Y.5    Ho, J.C.6
  • 23
    • 42049109549 scopus 로고    scopus 로고
    • Crag regulates epithelial architecture and polarized deposition of basement membrane proteins in Drosophila
    • PMID:18331716; DOI:10.1016/j.devcel.2007.12.012
    • DenefN, ChenY, WeeksSD, BarceloG, SchüpbachT. Crag regulates epithelial architecture and polarized deposition of basement membrane proteins in Drosophila. Dev Cell2008; 14:354-364; PMID:18331716; DOI:10.1016/j.devcel.2007.12.012.
    • (2008) Dev Cell , vol.14 , pp. 354-364
    • Denef, N.1    Chen, Y.2    Weeks, S.D.3    Barcelo, G.4    Schüpbach, T.5
  • 24
    • 84871691612 scopus 로고    scopus 로고
    • Crag is a GEF for Rab11 required for rhodopsin trafficking and maintenance of adult photoreceptor cells
    • PMID:23226104; DOI:10.1371/journal.pbio.1001438
    • XiongB, BayatV, JaiswalM, ZhangK, SandovalH, CharngWL, et al. Crag is a GEF for Rab11 required for rhodopsin trafficking and maintenance of adult photoreceptor cells. PLoS Biol2012; 10:e1001438; PMID:23226104; DOI:10.1371/journal.pbio.1001438.
    • (2012) PLoS Biol , vol.10
    • Xiong, B.1    Bayat, V.2    Jaiswal, M.3    Zhang, K.4    Sandoval, H.5    Charng, W.L.6
  • 25
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • PMID:15980461; DOI:10.1093/nar/gki408
    • SödingJ, BiegertA, LupasAN. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res2005; 33:W244-W248; PMID:15980461; DOI:10.1093/nar/gki408.
    • (2005) Nucleic Acids Res , vol.33
    • Söding, J.1    Biegert, A.2    Lupas, A.N.3
  • 26
    • 84874266850 scopus 로고    scopus 로고
    • Discovery of Novel DENN Proteins: Implications for the Evolution of Eukaryotic Intracellular Membrane Structures and Human Disease
    • PMID:23248642; DOI:10.3389/fgene.2012.00283
    • ZhangD, IyerLM, HeF, AravindL. Discovery of Novel DENN Proteins: Implications for the Evolution of Eukaryotic Intracellular Membrane Structures and Human Disease. Front Genet2012; 3:283; PMID:23248642; DOI:10.3389/fgene.2012.00283.
    • (2012) Front Genet , vol.3 , pp. 283
    • Zhang, D.1    Iyer, L.M.2    He, F.3    Aravind, L.4
  • 27
    • 84874246696 scopus 로고    scopus 로고
    • The product of C9orf72, a gene strongly implicated in neurodegeneration, is structurally related to DENN Rab-GEFs
    • PMID:23329412; DOI:10.1093/bioinformatics/bts725
    • LevineTP, DanielsRD, GattaAT, WongLH, HayesMJ. The product of C9orf72, a gene strongly implicated in neurodegeneration, is structurally related to DENN Rab-GEFs. Bioinformatics2013; 29:499-503; PMID:23329412; DOI:10.1093/bioinformatics/bts725.
    • (2013) Bioinformatics , vol.29 , pp. 499-503
    • Levine, T.P.1    Daniels, R.D.2    Gatta, A.T.3    Wong, L.H.4    Hayes, M.J.5
  • 28
    • 84861226898 scopus 로고    scopus 로고
    • Recent advances in the genetics of the ALS-FTLD complex
    • PMID:22477152; DOI:10.1007/s11910-012-0268-5
    • MorrisHR, WaiteAJ, WilliamsNM, NealJW, BlakeDJ. Recent advances in the genetics of the ALS-FTLD complex. Curr Neurol Neurosci Rep2012; 12:243-250; PMID:22477152; DOI:10.1007/s11910-012-0268-5.
    • (2012) Curr Neurol Neurosci Rep , vol.12 , pp. 243-250
    • Morris, H.R.1    Waite, A.J.2    Williams, N.M.3    Neal, J.W.4    Blake, D.J.5
  • 29
    • 33751109759 scopus 로고    scopus 로고
    • Longin-like folds identified in CHiPS and DUF254 proteins: Vesicle trafficking complexes conserved in eukaryotic evolution
    • PMID:17075139; DOI:10.1110/ps.062419006
    • KinchLN, GrishinNV. Longin-like folds identified in CHiPS and DUF254 proteins: vesicle trafficking complexes conserved in eukaryotic evolution. Protein Sci2006; 15:2669-2674; PMID:17075139; DOI:10.1110/ps.062419006.
    • (2006) Protein Sci , vol.15 , pp. 2669-2674
    • Kinch, L.N.1    Grishin, N.V.2
  • 30
    • 77957231342 scopus 로고    scopus 로고
    • The Mon1-Ccz1 complex is the GEF of the late endosomal Rab7 homolog Ypt7
    • PMID:20797862; DOI:10.1016/j.cub.2010.08.002
    • NordmannM, CabreraM, PerzA, BröckerC, OstrowiczC, Engelbrecht-VandréS, et al. The Mon1-Ccz1 complex is the GEF of the late endosomal Rab7 homolog Ypt7. Curr Biol2010; 20:1654-1659; PMID:20797862; DOI:10.1016/j.cub.2010.08.002.
    • (2010) Curr Biol , vol.20 , pp. 1654-1659
    • Nordmann, M.1    Cabrera, M.2    Perz, A.3    Bröcker, C.4    Ostrowicz, C.5    Engelbrecht-Vandré, S.6
  • 31
    • 84871875693 scopus 로고    scopus 로고
    • A divalent interaction between HPS1 and HPS4 is required for the formation of the biogenesis of lysosome-related organelle complex-3 (BLOC-3)
    • PMID:23103514; DOI:10.1016/j.bbamcr.2012.10.019
    • Carmona-RiveraC, SimeonovDR, CardilloND, GahlWA, CadillaCL. A divalent interaction between HPS1 and HPS4 is required for the formation of the biogenesis of lysosome-related organelle complex-3 (BLOC-3). Biochim Biophys Acta2013; 1833:468-478; PMID:23103514; DOI:10.1016/j.bbamcr.2012.10.019.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 468-478
    • Carmona-Rivera, C.1    Simeonov, D.R.2    Cardillo, N.D.3    Gahl, W.A.4    Cadilla, C.L.5
  • 32
    • 84865125882 scopus 로고    scopus 로고
    • Nprl3 is required for normal development of the cardiovascular system
    • PMID:22538705; DOI:10.1007/s00335-012-9398-y
    • KowalczykMS, HughesJR, BabbsC, Sanchez-PulidoL, SzumskaD, SharpeJA, et al. Nprl3 is required for normal development of the cardiovascular system. Mamm Genome2012; 23:404-415; PMID:22538705; DOI:10.1007/s00335-012-9398-y.
    • (2012) Mamm Genome , vol.23 , pp. 404-415
    • Kowalczyk, M.S.1    Hughes, J.R.2    Babbs, C.3    Sanchez-Pulido, L.4    Szumska, D.5    Sharpe, J.A.6
  • 33
    • 67651235863 scopus 로고    scopus 로고
    • A genome-wide screen for regulators of TORC1 in response to amino acid starvation reveals a conserved Npr2/3 complex
    • PMID:19521502; DOI:10.1371/journal.pgen.1000515
    • NeklesaTK, DavisRW. A genome-wide screen for regulators of TORC1 in response to amino acid starvation reveals a conserved Npr2/3 complex. PLoS Genet2009; 5:e1000515; PMID:19521502; DOI:10.1371/journal.pgen.1000515.
    • (2009) PLoS Genet , vol.5
    • Neklesa, T.K.1    Davis, R.W.2
  • 34
    • 79957971892 scopus 로고    scopus 로고
    • A conserved coatomer-related complex containing Sec13 and Seh1 dynamically associates with the vacuole in Saccharomyces cerevisiae
    • 006478; PMID:21454883; DOI:10.1074/mcp.M110.006478
    • DokudovskayaS, WaharteF, SchlessingerA, PieperU, DevosDP, CristeaIM, et al. A conserved coatomer-related complex containing Sec13 and Seh1 dynamically associates with the vacuole in Saccharomyces cerevisiae. Mol Cell Proteomics2011; 10:M110-, 006478; PMID:21454883; DOI:10.1074/mcp.M110.006478.
    • (2011) Mol Cell Proteomics , vol.10
    • Dokudovskaya, S.1    Waharte, F.2    Schlessinger, A.3    Pieper, U.4    Devos, D.P.5    Cristea, I.M.6
  • 35
    • 80655144720 scopus 로고    scopus 로고
    • Selective regulation of autophagy by the Iml1-Npr2-Npr3 complex in the absence of nitrogen starvation
    • PMID:21900499; DOI:10.1091/mbc.E11-06-0525
    • WuX, TuBP. Selective regulation of autophagy by the Iml1-Npr2-Npr3 complex in the absence of nitrogen starvation. Mol Biol Cell2011; 22:4124-4133; PMID:21900499; DOI:10.1091/mbc.E11-06-0525.
    • (2011) Mol Biol Cell , vol.22 , pp. 4124-4133
    • Wu, X.1    Tu, B.P.2
  • 36
    • 77951768486 scopus 로고    scopus 로고
    • Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
    • PMID:20381137; DOI:10.1016/j.cell.2010.02.024
    • SancakY, Bar-PeledL, ZoncuR, MarkhardAL, NadaS, SabatiniDM. Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell2010; 141:290-303; PMID:20381137; DOI:10.1016/j.cell.2010.02.024.
    • (2010) Cell , vol.141 , pp. 290-303
    • Sancak, Y.1    Bar-Peled, L.2    Zoncu, R.3    Markhard, A.L.4    Nada, S.5    Sabatini, D.M.6
  • 37
    • 84866431363 scopus 로고    scopus 로고
    • Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1
    • PMID:22980980; DOI:10.1016/j.cell.2012.07.032
    • Bar-PeledL, SchweitzerLD, ZoncuR, SabatiniDM. Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1. Cell2012; 150:1196-1208; PMID:22980980; DOI:10.1016/j.cell.2012.07.032.
    • (2012) Cell , vol.150 , pp. 1196-1208
    • Bar-Peled, L.1    Schweitzer, L.D.2    Zoncu, R.3    Sabatini, D.M.4
  • 38
    • 77956740779 scopus 로고    scopus 로고
    • Structural conservation of components in the amino acid sensing branch of the TOR pathway in yeast and mammals
    • PMID:20655927; DOI:10.1016/j.jmb.2010.07.034
    • KoganK, SpearED, KaiserCA, FassD. Structural conservation of components in the amino acid sensing branch of the TOR pathway in yeast and mammals. J Mol Biol2010; 402:388-398; PMID:20655927; DOI:10.1016/j.jmb.2010.07.034.
    • (2010) J Mol Biol , vol.402 , pp. 388-398
    • Kogan, K.1    Spear, E.D.2    Kaiser, C.A.3    Fass, D.4
  • 40
    • 77954568867 scopus 로고    scopus 로고
    • The crystal structure of dynein intermediate chain-light chain roadblock complex gives new insights into dynein assembly
    • PMID:20472935; DOI:10.1074/jbc.M110.103861
    • HallJ, SongY, KarplusPA, BarbarE. The crystal structure of dynein intermediate chain-light chain roadblock complex gives new insights into dynein assembly. J Biol Chem2010; 285:22566-22575; PMID:20472935; DOI:10.1074/jbc.M110.103861.
    • (2010) J Biol Chem , vol.285 , pp. 22566-22575
    • Hall, J.1    Song, Y.2    Karplus, P.A.3    Barbar, E.4
  • 41
    • 77958487311 scopus 로고    scopus 로고
    • TRAPP complexes in membrane traffic: Convergence through a common Rab
    • PMID:20966969; DOI:10.1038/nrm2999
    • BarrowmanJ, BhandariD, ReinischK, Ferro-NovickS. TRAPP complexes in membrane traffic: convergence through a common Rab. Nat Rev Mol Cell Biol2010; 11:759-763; PMID:20966969; DOI:10.1038/nrm2999.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 759-763
    • Barrowman, J.1    Bhandari, D.2    Reinisch, K.3    Ferro-Novick, S.4
  • 42
    • 79959257560 scopus 로고    scopus 로고
    • C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early stage in ER-to-Golgi trafficking
    • PMID:21525244; DOI:10.1091/mbc.E10-11-0873
    • ScrivensPJ, NoueihedB, ShahrzadN, HulS, BrunetS, SacherM. C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early stage in ER-to-Golgi trafficking. Mol Biol Cell2011; 22:2083-2093; PMID:21525244; DOI:10.1091/mbc.E10-11-0873.
    • (2011) Mol Biol Cell , vol.22 , pp. 2083-2093
    • Scrivens, P.J.1    Noueihed, B.2    Shahrzad, N.3    Hul, S.4    Brunet, S.5    Sacher, M.6
  • 43
    • 33847648364 scopus 로고    scopus 로고
    • Control systems for membrane fusion in the ancestral eukaryote; evolution of tethering complexes and SM proteins
    • PMID:17319956; DOI:10.1186/1471-2148-7-29
    • KoumandouVL, DacksJB, CoulsonRM, FieldMC. Control systems for membrane fusion in the ancestral eukaryote; evolution of tethering complexes and SM proteins. BMC Evol Biol2007; 7:29; PMID:17319956; DOI:10.1186/1471-2148-7-29.
    • (2007) BMC Evol Biol , vol.7 , pp. 29
    • Koumandou, V.L.1    Dacks, J.B.2    Coulson, R.M.3    Field, M.C.4
  • 44
    • 79955737985 scopus 로고    scopus 로고
    • Organization and assembly of the TRAPPII complex
    • PMID:21453443; DOI:10.1111/j.1600-0854.2011.01181.x
    • ChoiC, DaveyM, SchluterC, PandherP, FangY, FosterLJ, et al. Organization and assembly of the TRAPPII complex. Traffic2011; 12:715-725; PMID:21453443; DOI:10.1111/j.1600-0854.2011.01181.x.
    • (2011) Traffic , vol.12 , pp. 715-725
    • Choi, C.1    Davey, M.2    Schluter, C.3    Pandher, P.4    Fang, Y.5    Foster, L.J.6
  • 45
    • 33750799403 scopus 로고    scopus 로고
    • The architecture of the multisubunit TRAPP I complex suggests a model for vesicle tethering
    • PMID:17110339; DOI:10.1016/j.cell.2006.09.029
    • KimYG, RaunserS, MungerC, WagnerJ, SongYL, CyglerM, et al. The architecture of the multisubunit TRAPP I complex suggests a model for vesicle tethering. Cell2006; 127:817-830; PMID:17110339; DOI:10.1016/j.cell.2006.09.029.
    • (2006) Cell , vol.127 , pp. 817-830
    • Kim, Y.G.1    Raunser, S.2    Munger, C.3    Wagner, J.4    Song, Y.L.5    Cygler, M.6
  • 46
    • 77956286311 scopus 로고    scopus 로고
    • SEDLIN forms homodimers: Characterisation of SEDLIN mutations and their interactions with transcription factors MBP1, PITX1 and SF1
    • PMID:20498720; DOI:10.1371/journal.pone.0010646
    • JeyabalanJ, NesbitMA, GalvanovskisJ, CallaghanR, RorsmanP, ThakkerRV. SEDLIN forms homodimers: characterisation of SEDLIN mutations and their interactions with transcription factors MBP1, PITX1 and SF1. PLoS One2010; 5:e10646; PMID:20498720; DOI:10.1371/journal.pone.0010646.
    • (2010) PLoS One , vol.5
    • Jeyabalan, J.1    Nesbit, M.A.2    Galvanovskis, J.3    Callaghan, R.4    Rorsman, P.5    Thakker, R.V.6
  • 47
    • 84866759304 scopus 로고    scopus 로고
    • Sedlin controls the ER export of procollagen by regulating the Sar1 cycle
    • PMID:23019651; DOI:10.1126/science.1224947
    • VendittiR, ScanuT, SantoroM, Di TullioG, SpaarA, GaibissoR, et al. Sedlin controls the ER export of procollagen by regulating the Sar1 cycle. Science2012; 337:1668-1672; PMID:23019651; DOI:10.1126/science.1224947.
    • (2012) Science , vol.337 , pp. 1668-1672
    • Venditti, R.1    Scanu, T.2    Santoro, M.3    Di Tullio, G.4    Spaar, A.5    Gaibisso, R.6
  • 48
    • 80051693767 scopus 로고    scopus 로고
    • The adaptor function of TRAPPC2 in mammalian TRAPPs explains TRAPPC2-associated SEDT and TRAPPC9-associated congenital intellectual disability
    • PMID:21858081; DOI:10.1371/journal.pone.0023350
    • ZongM, WuXG, ChanCW, ChoiMY, ChanHC, TannerJA, et al. The adaptor function of TRAPPC2 in mammalian TRAPPs explains TRAPPC2-associated SEDT and TRAPPC9-associated congenital intellectual disability. PLoS One2011; 6:e23350; PMID:21858081; DOI:10.1371/journal.pone.0023350.
    • (2011) PLoS One , vol.6
    • Zong, M.1    Wu, X.G.2    Chan, C.W.3    Choi, M.Y.4    Chan, H.C.5    Tanner, J.A.6
  • 49
    • 78549254476 scopus 로고    scopus 로고
    • Molecular architecture of the TRAPPII complex and implications for vesicle tethering
    • PMID:20972447; DOI:10.1038/nsmb.1914
    • YipCK, BerscheminskiJ, WalzT. Molecular architecture of the TRAPPII complex and implications for vesicle tethering. Nat Struct Mol Biol2010; 17:1298-1304; PMID:20972447; DOI:10.1038/nsmb.1914.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1298-1304
    • Yip, C.K.1    Berscheminski, J.2    Walz, T.3
  • 50
    • 0033638091 scopus 로고    scopus 로고
    • The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32
    • PMID:11102533
    • JonesS, NewmanC, LiuF, SegevN. The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32. Mol Biol Cell2000; 11:4403-4411; PMID:11102533.
    • (2000) Mol Biol Cell , vol.11 , pp. 4403-4411
    • Jones, S.1    Newman, C.2    Liu, F.3    Segev, N.4
  • 51
    • 84862552255 scopus 로고    scopus 로고
    • Modular TRAPP complexes regulate intracellular protein trafficking through multiple Ypt/Rab GTPases in Saccharomyces cerevisiae
    • PMID:22426882; DOI:10.1534/genetics.112.139378
    • ZouS, LiuY, ZhangXQ, ChenY, YeM, ZhuX, et al. Modular TRAPP complexes regulate intracellular protein trafficking through multiple Ypt/Rab GTPases in Saccharomyces cerevisiae. Genetics2012; 191:451-460; PMID:22426882; DOI:10.1534/genetics.112.139378.
    • (2012) Genetics , vol.191 , pp. 451-460
    • Zou, S.1    Liu, Y.2    Zhang, X.Q.3    Chen, Y.4    Ye, M.5    Zhu, X.6
  • 52
    • 0034676094 scopus 로고    scopus 로고
    • TRAPP stimulates guanine nucleotide exchange on Ypt1p
    • PMID:11038176; DOI:10.1083/jcb.151.2.289
    • WangW, SacherM, Ferro-NovickS. TRAPP stimulates guanine nucleotide exchange on Ypt1p. J Cell Biol2000; 151:289-296; PMID:11038176; DOI:10.1083/jcb.151.2.289.
    • (2000) J Cell Biol , vol.151 , pp. 289-296
    • Wang, W.1    Sacher, M.2    Ferro-Novick, S.3
  • 53
    • 80053353907 scopus 로고    scopus 로고
    • Trs65p, a subunit of the Ypt1p GEF TRAPPII, interacts with the Arf1p exchange factor Gea2p to facilitate COPI-mediated vesicle traffic
    • PMID:21813735; DOI:10.1091/mbc.E11-03-0197
    • ChenS, CaiH, ParkSK, MenonS, JacksonCL, Ferro-NovickS. Trs65p, a subunit of the Ypt1p GEF TRAPPII, interacts with the Arf1p exchange factor Gea2p to facilitate COPI-mediated vesicle traffic. Mol Biol Cell2011; 22:3634-3644; PMID:21813735; DOI:10.1091/mbc.E11-03-0197.
    • (2011) Mol Biol Cell , vol.22 , pp. 3634-3644
    • Chen, S.1    Cai, H.2    Park, S.K.3    Menon, S.4    Jackson, C.L.5    Ferro-Novick, S.6
  • 54
    • 57749191527 scopus 로고    scopus 로고
    • Crystal structure of human synbindin reveals two conformations of longin domain
    • PMID:18466758; DOI:10.1016/j.bbrc.2008.04.143
    • FanS, WeiZ, XuH, GongW. Crystal structure of human synbindin reveals two conformations of longin domain. Biochem Biophys Res Commun2009; 378:338-343; PMID:18466758; DOI:10.1016/j.bbrc.2008.04.143.
    • (2009) Biochem Biophys Res Commun , vol.378 , pp. 338-343
    • Fan, S.1    Wei, Z.2    Xu, H.3    Gong, W.4


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