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Volumn 14, Issue 4, 2002, Pages 506-514

Organelle identity and the targeting of peripheral membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; DIACYLGLYCEROL; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE; LIPID; MEMBRANE PROTEIN; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL KINASE; PHOSPHOLIPID; RAB PROTEIN;

EID: 0036701891     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(02)00350-2     Document Type: Review
Times cited : (55)

References (84)
  • 1
    • 0035575616 scopus 로고    scopus 로고
    • Rab GTPases: Specifying and deciphering organelle identity and function
    • Pfeffer S.R. Rab GTPases: specifying and deciphering organelle identity and function. Trends Cell Biol. 11:2001;487-491.
    • (2001) Trends Cell Biol , vol.11 , pp. 487-491
    • Pfeffer, S.R.1
  • 2
    • 0035425411 scopus 로고    scopus 로고
    • Ypt and Rab GTPases: Insight into functions through novel interactions
    • Segev N. Ypt and Rab GTPases: insight into functions through novel interactions. Curr Opin Cell Biol. 13:2001;500-511.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 500-511
    • Segev, N.1
  • 4
    • 0033937941 scopus 로고    scopus 로고
    • Regulators and effectors of the ARF GTPases
    • Donaldson J.G., Jackson C.L. Regulators and effectors of the ARF GTPases. Curr Opin Cell Biol. 12:2000;475-482.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 475-482
    • Donaldson, J.G.1    Jackson, C.L.2
  • 5
    • 0035890324 scopus 로고    scopus 로고
    • Functional and physical interactions of the adaptor protein complex AP-4 with ADP-ribosylation factors (ARFs)
    • Boehm M., Aguilar R.C., Bonifacino J.S. Functional and physical interactions of the adaptor protein complex AP-4 with ADP-ribosylation factors (ARFs). EMBO J. 20:2001;6265-6276.
    • (2001) EMBO J , vol.20 , pp. 6265-6276
    • Boehm, M.1    Aguilar, R.C.2    Bonifacino, J.S.3
  • 6
    • 0035815302 scopus 로고    scopus 로고
    • The GGAs promote ARF-dependent recruitment of clathrin to the TGN
    • Puertollano R., Randazzo P.A., Presley J.F., Hartnell L.M., Bonifacino J.S. The GGAs promote ARF-dependent recruitment of clathrin to the TGN. Cell. 105:2001;93-102. GGAs are one of the subunits of clathrin-containing coats found on the Golgi. This paper shows that the targeting of GGAs, and their clathrin vesicle coats, to the Golgi is mediated by direct binding to the GTP form of the GTPase ADP-ribosylation factor 1.
    • (2001) Cell , vol.105 , pp. 93-102
    • Puertollano, R.1    Randazzo, P.A.2    Presley, J.F.3    Hartnell, L.M.4    Bonifacino, J.S.5
  • 7
    • 0034752915 scopus 로고    scopus 로고
    • GGA proteins: New players in the sorting game
    • Boman A.L. GGA proteins: new players in the sorting game. J Cell Sci. 114:2001;3413-3418.
    • (2001) J Cell Sci , vol.114 , pp. 3413-3418
    • Boman, A.L.1
  • 8
    • 0033950864 scopus 로고    scopus 로고
    • Turning on ARF: The Sec7 family of guanine-nucleotide-exchange factors
    • Jackson C.L., Casanova J.E. Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors. Trends Cell Biol. 10:2000;60-67.
    • (2000) Trends Cell Biol , vol.10 , pp. 60-67
    • Jackson, C.L.1    Casanova, J.E.2
  • 9
    • 0034943777 scopus 로고    scopus 로고
    • The ARF exchange factors Gea1p and Gea2p regulate Golgi structure and function in yeast
    • Peyroche A., Courbeyrette R., Rambourg A., Jackson C.L. The ARF exchange factors Gea1p and Gea2p regulate Golgi structure and function in yeast. J Cell Sci. 114:2001;2241-2253.
    • (2001) J Cell Sci , vol.114 , pp. 2241-2253
    • Peyroche, A.1    Courbeyrette, R.2    Rambourg, A.3    Jackson, C.L.4
  • 10
    • 0036151274 scopus 로고    scopus 로고
    • Localization of large ADP-ribosylation factor guanine nucleotide exchange factors to different Golgi compartments: Evidence for distinct functions in protein traffic
    • Zhao X., Lasell T.K., Melancon P. Localization of large ADP-ribosylation factor guanine nucleotide exchange factors to different Golgi compartments: evidence for distinct functions in protein traffic. Mol Biol Cell. 13:2002;119-133.
    • (2002) Mol Biol Cell , vol.13 , pp. 119-133
    • Zhao, X.1    Lasell, T.K.2    Melancon, P.3
  • 11
    • 0037088675 scopus 로고    scopus 로고
    • Overexpression of an ADP-ribosylation factor-guanine nucleotide exchange factor, BIG2, uncouples brefeldin A-induced adaptor protein-1 coat dissociation and membrane tubulation
    • Shinotsuka C., Yoshida Y., Kawamoto K., Takatsu H., Nakayama K. Overexpression of an ADP-ribosylation factor-guanine nucleotide exchange factor, BIG2, uncouples brefeldin A-induced adaptor protein-1 coat dissociation and membrane tubulation. J Biol Chem. 277:2002;9468-9473. Two classes of Sec7 domain guanine nucleotide exchange factors for ADP-ribosylation factor (ARF) have been found on the Golgi apparatus. Overexpression of one (BIG2) prevents the brefeldin-A-induced redistribution of the AP1 clathrin adaptor, but not of coat protein complex I. This suggests that targeting of BIG2 is restricted to just the trans side of the Golgi.
    • (2002) J Biol Chem , vol.277 , pp. 9468-9473
    • Shinotsuka, C.1    Yoshida, Y.2    Kawamoto, K.3    Takatsu, H.4    Nakayama, K.5
  • 12
    • 0033529249 scopus 로고    scopus 로고
    • P200 ARF-GEP1: A Golgi-localized guanine nucleotide exchange protein whose Sec7 domain is targeted by the drug brefeldin A
    • Mansour S.J., Skaug J., Zhao X.H., Giordano J., Scherer S.W., Melancon P. p200 ARF-GEP1: a Golgi-localized guanine nucleotide exchange protein whose Sec7 domain is targeted by the drug brefeldin A. Proc Natl Acad Sci USA. 96:1999;7968-7973.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 7968-7973
    • Mansour, S.J.1    Skaug, J.2    Zhao, X.H.3    Giordano, J.4    Scherer, S.W.5    Melancon, P.6
  • 13
    • 0002955384 scopus 로고    scopus 로고
    • Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: Involvement of specific residues of the Sec7 domain
    • Peyroche A., Antonny B., Robineau S., Acker J., Cherfils J., Jackson C.L. Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain. Mol Cell. 3:1999;275-285.
    • (1999) Mol Cell , vol.3 , pp. 275-285
    • Peyroche, A.1    Antonny, B.2    Robineau, S.3    Acker, J.4    Cherfils, J.5    Jackson, C.L.6
  • 14
    • 0037169078 scopus 로고    scopus 로고
    • A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes
    • Nagai H., Kagan J.C., Zhu X., Kahn R.A., Roy C.R. A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes. Science. 295:2002;679-682. This work demonstrates that a bacterially encoded protein can activate ADP ribosylation factors (ARFs) in vitro, and in vivo causes the recruitment of ARF1 to phagosomes. However, at present only the bacteria know why they do this, as deletion of the gene has no effect on replication in diverse hosts.
    • (2002) Science , vol.295 , pp. 679-682
    • Nagai, H.1    Kagan, J.C.2    Zhu, X.3    Kahn, R.A.4    Roy, C.R.5
  • 15
    • 0035933796 scopus 로고    scopus 로고
    • ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: Characterizing ARL1-binding proteins
    • Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A. ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1-binding proteins. J Biol Chem. 276:2001;22826-22837.
    • (2001) J Biol Chem , vol.276 , pp. 22826-22837
    • Van Valkenburgh, H.1    Shern, J.F.2    Sharer, J.D.3    Zhu, X.4    Kahn, R.A.5
  • 16
    • 0035975972 scopus 로고    scopus 로고
    • Cell motility: ARNO and ARF6 at the cutting edge
    • Turner C.E., Brown M.C. Cell motility: ARNO and ARF6 at the cutting edge. Curr Biol. 11:2001;R875-R877.
    • (2001) Curr Biol , vol.11
    • Turner, C.E.1    Brown, M.C.2
  • 17
    • 0034735952 scopus 로고    scopus 로고
    • Membrane targeting: What a difference a G makes
    • Cullen P.J., Chardin P. Membrane targeting: what a difference a G makes. Curr Biol. 10:2000;R876-R878.
    • (2000) Curr Biol , vol.10
    • Cullen, P.J.1    Chardin, P.2
  • 18
    • 0036137684 scopus 로고    scopus 로고
    • Rab GTPases, intracellular traffic and disease
    • Seabra M.C., Mules E.H., Hume A.N. Rab GTPases, intracellular traffic and disease. Trends Mol Med. 8:2002;23-30.
    • (2002) Trends Mol Med , vol.8 , pp. 23-30
    • Seabra, M.C.1    Mules, E.H.2    Hume, A.N.3
  • 19
  • 21
    • 0034735539 scopus 로고    scopus 로고
    • New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion
    • Wurmser A.E., Sato T.K., Emr S.D. New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion. J Cell Biol. 151:2000;551-562.
    • (2000) J Cell Biol , vol.151 , pp. 551-562
    • Wurmser, A.E.1    Sato, T.K.2    Emr, S.D.3
  • 23
    • 0036226156 scopus 로고    scopus 로고
    • Identification of an organelle receptor for myosin-Va
    • Wu X.S., Rao K., Zhang H., Wang F., Sellers J.R., Matesic L.E., Copeland N.G., Jenkins N.A., Hammer J.A. I.I.I. Identification of an organelle receptor for myosin-Va. Nat Cell Biol. 4:2002;271-278. Rab27a is found on melanosomes, and this paper, and Fukuda et al. (2002) [24••] below, show that the protein melanophilin binds the Rab at one end and myosin Va at the other, thereby linking motor to organelle.
    • (2002) Nat Cell Biol , vol.4 , pp. 271-278
    • Wu, X.S.1    Rao, K.2    Zhang, H.3    Wang, F.4    Sellers, J.R.5    Matesic, L.E.6    Copeland, N.G.7    Jenkins, N.A.8    Hammer J.A., I.I.I.9
  • 24
    • 0037023745 scopus 로고    scopus 로고
    • Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: Implications of a tripartite protein complex for melanosome transport
    • Fukuda M., Kuroda T.S., Mikoshiba K. Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: implications of a tripartite protein complex for melanosome transport. J Biol Chem. 277:2002;12432-12436. See annotation Wu et al. (2002) [23••] .
    • (2002) J Biol Chem , vol.277 , pp. 12432-12436
    • Fukuda, M.1    Kuroda, T.S.2    Mikoshiba, K.3
  • 26
    • 0025948794 scopus 로고
    • Hypervariable C-terminal domain of Rab proteins acts as a targeting signal
    • Chavrier P., Gorvel J.P., Stelzer E., Simons K., Gruenberg J., Zerial M. Hypervariable C-terminal domain of Rab proteins acts as a targeting signal. Nature. 353:1991;769-772.
    • (1991) Nature , vol.353 , pp. 769-772
    • Chavrier, P.1    Gorvel, J.P.2    Stelzer, E.3    Simons, K.4    Gruenberg, J.5    Zerial, M.6
  • 28
    • 0036298325 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Pra1p/Yip3p interacts with Yip1p and Rab proteins
    • Calero M., Collins R.N. Saccharomyces cerevisiae Pra1p/Yip3p interacts with Yip1p and Rab proteins. Biochem Biophys Res Commun. 290:2002;676-681.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 676-681
    • Calero, M.1    Collins, R.N.2
  • 29
    • 0035958898 scopus 로고    scopus 로고
    • Prenylated Rab acceptor protein is a receptor for prenylated small GTPases
    • Figueroa C., Taylor J., Vojtek A.B. Prenylated Rab acceptor protein is a receptor for prenylated small GTPases. J Biol Chem. 276:2001;28219-28225.
    • (2001) J Biol Chem , vol.276 , pp. 28219-28225
    • Figueroa, C.1    Taylor, J.2    Vojtek, A.B.3
  • 30
    • 0034282521 scopus 로고    scopus 로고
    • A novel Golgi membrane protein is part of a GTPase-binding protein complex involved in vesicle targeting
    • Matern H., Yang X., Andrulis E., Sternglanz R., Trepte H.H., Gallwitz D. A novel Golgi membrane protein is part of a GTPase-binding protein complex involved in vesicle targeting. EMBO J. 19:2000;4485-4492.
    • (2000) EMBO J , vol.19 , pp. 4485-4492
    • Matern, H.1    Yang, X.2    Andrulis, E.3    Sternglanz, R.4    Trepte, H.H.5    Gallwitz, D.6
  • 32
    • 0033598138 scopus 로고    scopus 로고
    • The missing (L) UNC?
    • Raff J.W. The missing (L) UNC? Curr Biol. 9:1999;R708-R710.
    • (1999) Curr Biol , vol.9
    • Raff, J.W.1
  • 33
    • 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. 12:2001;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
  • 34
    • 0034665261 scopus 로고    scopus 로고
    • Ric1p and Rgp1p form a complex that catalyses nucleotide exchange on Ypt6p
    • Siniossoglou S., Peak-Chew S.Y., Pelham H.R. Ric1p and Rgp1p form a complex that catalyses nucleotide exchange on Ypt6p. EMBO J. 19:2000;4885-4894.
    • (2000) EMBO J , vol.19 , pp. 4885-4894
    • Siniossoglou, S.1    Peak-Chew, S.Y.2    Pelham, H.R.3
  • 35
    • 17944372902 scopus 로고    scopus 로고
    • GRAB: A physiologic guanine nucleotide exchange factor for Rab3A, which interacts with inositol hexakisphosphate kinase
    • Luo H.R., Saiardi A., Nagata E., Ye K., Yu H., Jung T.S., Luo X., Jain S., Sawa A., Snyder S.H. GRAB: a physiologic guanine nucleotide exchange factor for Rab3A, which interacts with inositol hexakisphosphate kinase. Neuron. 31:2001;439-451.
    • (2001) Neuron , vol.31 , pp. 439-451
    • Luo, H.R.1    Saiardi, A.2    Nagata, E.3    Ye, K.4    Yu, H.5    Jung, T.S.6    Luo, X.7    Jain, S.8    Sawa, A.9    Snyder, S.H.10
  • 36
    • 0035408008 scopus 로고    scopus 로고
    • Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide exchange activity of RIN1
    • Tall G.G., Barbieri M.A., Stahl P.D., Horazdovsky B.F. Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide exchange activity of RIN1. Dev Cell. 1:2001;73-82. A thorough characterisation of the Ras interacting protein RIN1 reveals it to be a guanine nucleotide exchange factor (GEF) for Rab5, thereby providing a link between activation of signal transduction and the subsequent endocytic events involved in receptor downregulation. RIN1 is related to VPS9, and Rabex5, and there are further related proteins in the human genome, suggesting a family of such GEFs.
    • (2001) Dev Cell , vol.1 , pp. 73-82
    • Tall, G.G.1    Barbieri, M.A.2    Stahl, P.D.3    Horazdovsky, B.F.4
  • 37
    • 0035424240 scopus 로고    scopus 로고
    • 2 regulation of surface membrane traffic
    • 2 regulation of surface membrane traffic. Curr Opin Cell Biol. 13:2001;493-499.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 493-499
    • Martin, T.F.1
  • 38
    • 0035313710 scopus 로고    scopus 로고
    • Subcellular targeting by membrane lipids
    • Hurley J.H., Meyer T. Subcellular targeting by membrane lipids. Curr Opin Cell Biol. 13:2001;146-152.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 146-152
    • Hurley, J.H.1    Meyer, T.2
  • 39
    • 0035172107 scopus 로고    scopus 로고
    • Sac1 lipid phosphatase and Stt4 phosphatidylinositol 4-kinase regulate a pool of phosphatidylinositol 4-phosphate that functions in the control of the actin cytoskeleton and vacuole morphology
    • Foti M., Audhya A., Emr S.D. Sac1 lipid phosphatase and Stt4 phosphatidylinositol 4-kinase regulate a pool of phosphatidylinositol 4-phosphate that functions in the control of the actin cytoskeleton and vacuole morphology. Mol Biol Cell. 12:2001;2396-2411.
    • (2001) Mol Biol Cell , vol.12 , pp. 2396-2411
    • Foti, M.1    Audhya, A.2    Emr, S.D.3
  • 40
    • 0033824820 scopus 로고    scopus 로고
    • A phospholipid kinase regulates actin organization and intercellular bridge formation during germline cytokinesis
    • Brill J.A., Hime G.R., Scharer-Schuksz M., Fuller M.T. A phospholipid kinase regulates actin organization and intercellular bridge formation during germline cytokinesis. Development. 127:2000;3855-3864. How do the flies do it? Mutant flies that apparently lack all phosphatidylinositol 4-OH kinase-β develop normally, and only show defects in spermatogenesis.
    • (2000) Development , vol.127 , pp. 3855-3864
    • Brill, J.A.1    Hime, G.R.2    Scharer-Schuksz, M.3    Fuller, M.T.4
  • 42
    • 0037085263 scopus 로고    scopus 로고
    • Stereo-specific substrate recognition by phosphatidylinositol phosphate kinases is swapped by changing a single amino acid residue
    • Kunz J., Fuelling A., Kolbe L., Anderson R.A. Stereo-specific substrate recognition by phosphatidylinositol phosphate kinases is swapped by changing a single amino acid residue. J Biol Chem. 277:2002;5611-5619.
    • (2002) J Biol Chem , vol.277 , pp. 5611-5619
    • Kunz, J.1    Fuelling, A.2    Kolbe, L.3    Anderson, R.A.4
  • 43
    • 0037197804 scopus 로고    scopus 로고
    • Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent, and independent, components
    • Levine T.P., Munro S. Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent, and independent, components. Curr Biol. 12:2002;695-704.
    • (2002) Curr Biol , vol.12 , pp. 695-704
    • Levine, T.P.1    Munro, S.2
  • 44
    • 0035782856 scopus 로고    scopus 로고
    • Intracellular trafficking and turnover of phosphatidylinositol 3-phosphate
    • Stenmark H., Gillooly D.J. Intracellular trafficking and turnover of phosphatidylinositol 3-phosphate. Semin Cell Dev Biol. 12:2001;193-199.
    • (2001) Semin Cell Dev Biol , vol.12 , pp. 193-199
    • Stenmark, H.1    Gillooly, D.J.2
  • 45
    • 0035930332 scopus 로고    scopus 로고
    • Multivalent endosome targeting by homodimeric EEA1
    • Dumas J.J., Merithew E., Sudharshan E., Rajamani D., Hayes S., Lawe D., Corvera S., Lambright D.G. Multivalent endosome targeting by homodimeric EEA1. Mol Cell. 8:2001;947-958. The structure of part of EEA1 reveals how this FYVE-domain protein binds to phosphatidylinositol 3-phosphate. It also provides a particularly clear account of the large effects on affinity and specificity that come from dimerising targeting domains.
    • (2001) Mol Cell , vol.8 , pp. 947-958
    • Dumas, J.J.1    Merithew, E.2    Sudharshan, E.3    Rajamani, D.4    Hayes, S.5    Lawe, D.6    Corvera, S.7    Lambright, D.G.8
  • 46
  • 47
    • 0037138361 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-phosphate-binding FYVE finger
    • Stenmark H., Aasland R., Driscoll P.C. The phosphatidylinositol 3-phosphate-binding FYVE finger. FEBS Lett. 513:2002;77-84.
    • (2002) FEBS Lett , vol.513 , pp. 77-84
    • Stenmark, H.1    Aasland, R.2    Driscoll, P.C.3
  • 48
    • 0035899829 scopus 로고    scopus 로고
    • A PtdIns(3)P-specific probe cycles on and off host cell membranes during Salmonella invasion of mammalian cells
    • Pattni K., Jepson M., Stenmark H., Banting G. A PtdIns(3)P-specific probe cycles on and off host cell membranes during Salmonella invasion of mammalian cells. Curr Biol. 11:2001;1636-1642.
    • (2001) Curr Biol , vol.11 , pp. 1636-1642
    • Pattni, K.1    Jepson, M.2    Stenmark, H.3    Banting, G.4
  • 52
    • 0035032723 scopus 로고    scopus 로고
    • Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network
    • Kihara A., Kabeya Y., Ohsumi Y., Yoshimori T. Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network. EMBO Rep. 2:2001;330-335. See annotation Kihara et al. (2001) [55••].
    • (2001) EMBO Rep , vol.2 , pp. 330-335
    • Kihara, A.1    Kabeya, Y.2    Ohsumi, Y.3    Yoshimori, T.4
  • 53
    • 0026086456 scopus 로고
    • A genetic and structural analysis of the yeast Vps15 protein kinase: Evidence for a direct role of Vps15p in vacuolar protein delivery
    • Herman P.K., Stack J.H., Emr S.D. A genetic and structural analysis of the yeast Vps15 protein kinase: evidence for a direct role of Vps15p in vacuolar protein delivery. EMBO J. 10:1991;4049-4060.
    • (1991) EMBO J , vol.10 , pp. 4049-4060
    • Herman, P.K.1    Stack, J.H.2    Emr, S.D.3
  • 55
    • 0035809160 scopus 로고    scopus 로고
    • Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae
    • Kihara A., Noda T., Ishihara N., Ohsumi Y. Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae. J Cell Biol. 152:2001;519-530. The phosphatidylinositol 3-kinase Vps34p has emerged as a key factor in organising the endocytic pathway. However, little is known about how the protein itself is targeted and regulated, and this paper provides clear evidence that in yeast it is a component of two large complexes. This opens the way to examining the functioning of the complexes, and also reveals that the kinase is involved in both endosomal sorting and autophagy. The general significance of these findings is increased by one of the subunits having a human homologue (see also Kihara et al. [2001] [52•] ).
    • (2001) J Cell Biol , vol.152 , pp. 519-530
    • Kihara, A.1    Noda, T.2    Ishihara, N.3    Ohsumi, Y.4
  • 56
    • 18244392475 scopus 로고    scopus 로고
    • Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices
    • Krugmann S., Anderson K.E., Ridley S.H., Risso N., McGregor A., Coadwell J., Davidson K., Eguinoa A., Ellson C.D., Lipp P., et al. Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices. Mol Cell. 9:2002;95-108. Many peripheral membrane proteins are recruited by binding phosphoinositides, and in a biochemical tour de force many new candidate effectors are identified by the use of phosphoinositide affinity columns.
    • (2002) Mol Cell , vol.9 , pp. 95-108
    • Krugmann, S.1    Anderson, K.E.2    Ridley, S.H.3    Risso, N.4    McGregor, A.5    Coadwell, J.6    Davidson, K.7    Eguinoa, A.8    Ellson, C.D.9    Lipp, P.10
  • 57
    • 0036181710 scopus 로고    scopus 로고
    • The yeast synaptojanin-like proteins control the cellular distribution of phosphatidylinositol (4,5)-bisphosphate
    • Stefan C.J., Audhya A., Emr S.D. The yeast synaptojanin-like proteins control the cellular distribution of phosphatidylinositol (4,5)-bisphosphate. Mol Biol Cell. 13:2002;542-557. This is a clear demonstration that phosphatidylinositol 4,5-bisphosphate is predominantly localised to the plasma membrane in yeast, and that at least one function of the synaptojanin-like lipid phosphatases is to prevent phosphatidylinositol 4,5-bisphosphate accumulating on internal membranes. In addition, the paper describes the Golgi targeting of a pleckstrin homology domain that is examined in detail in Levine and Munro (2002) [43] .
    • (2002) Mol Biol Cell , vol.13 , pp. 542-557
    • Stefan, C.J.1    Audhya, A.2    Emr, S.D.3
  • 58
    • 0028986620 scopus 로고
    • Protein kinase Cε is localized to the Golgi via its zinc-finger domain and modulates Golgi function
    • Lehel C., Olah Z., Jakab G., Anderson W.B. Protein kinase Cε is localized to the Golgi via its zinc-finger domain and modulates Golgi function. Proc Natl Acad Sci USA. 92:1995;1406-1410.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1406-1410
    • Lehel, C.1    Olah, Z.2    Jakab, G.3    Anderson, W.B.4
  • 59
    • 0035503293 scopus 로고    scopus 로고
    • Recruitment of protein kinase D to the trans-Golgi network via the first cysteine-rich domain
    • Maeda Y., Beznoussenko G.V., Van Lint J., Mironov A.A., Malhotra V. Recruitment of protein kinase D to the trans-Golgi network via the first cysteine-rich domain. EMBO J. 20:2001;5982-5990.
    • (2001) EMBO J , vol.20 , pp. 5982-5990
    • Maeda, Y.1    Beznoussenko, G.V.2    Van Lint, J.3    Mironov, A.A.4    Malhotra, V.5
  • 60
    • 0037033793 scopus 로고    scopus 로고
    • Structural requirements for localization and activation of protein kinase C μ (PKC μ) at the Golgi compartment
    • Hausser A., Link G., Bamberg L., Burzlaff A., Lutz S., Pfizenmaier K., Johannes F.J. Structural requirements for localization and activation of protein kinase C μ (PKC μ) at the Golgi compartment. J Cell Biol. 156:2002;65-74.
    • (2002) J Cell Biol , vol.156 , pp. 65-74
    • Hausser, A.1    Link, G.2    Bamberg, L.3    Burzlaff, A.4    Lutz, S.5    Pfizenmaier, K.6    Johannes, F.J.7
  • 61
    • 0024020409 scopus 로고
    • What is the fate of diacylglycerol produced at the Golgi apparatus?
    • Pagano R.E. What is the fate of diacylglycerol produced at the Golgi apparatus? Trends Biochem Sci. 13:1988;202-205.
    • (1988) Trends Biochem Sci , vol.13 , pp. 202-205
    • Pagano, R.E.1
  • 62
    • 0035830496 scopus 로고    scopus 로고
    • Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network
    • Liljedahl M., Maeda Y., Colanzi A., Ayala I., Van Lint J., Malhotra V. Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network. Cell. 104:2001;409-420. Overexpression of a kinase-defective form of protein kinase Cμ/protein kinase D has the dramatic effect of causing the late Golgi to form long tubules containing trans-Golgi network (TGN) markers and trapped exocytic cargo. This suggests that the kinase is required for normal exit from the mammalian TGN, although the absence of homologues in lower eukaryotes indicates that it may not always be obligatory.
    • (2001) Cell , vol.104 , pp. 409-420
    • Liljedahl, M.1    Maeda, Y.2    Colanzi, A.3    Ayala, I.4    Van Lint, J.5    Malhotra, V.6
  • 63
    • 0036161583 scopus 로고    scopus 로고
    • Electrostatic control of the membrane targeting of C2 domains
    • Murray D., Honig B. Electrostatic control of the membrane targeting of C2 domains. Mol Cell. 9:2002;145-154.
    • (2002) Mol Cell , vol.9 , pp. 145-154
    • Murray, D.1    Honig, B.2
  • 64
    • 0035977019 scopus 로고    scopus 로고
    • The role of electrostatic interactions in the regulation of the membrane association of G protein beta gamma heterodimers
    • Murray D., McLaughlin S., Honig B. The role of electrostatic interactions in the regulation of the membrane association of G protein beta gamma heterodimers. J Biol Chem. 276:2001;45153-45159.
    • (2001) J Biol Chem , vol.276 , pp. 45153-45159
    • Murray, D.1    McLaughlin, S.2    Honig, B.3
  • 65
    • 0029416828 scopus 로고
    • The ARF1 GTPase-activating protein: Zinc finger motif and Golgi complex localization
    • Cukierman E., Huber I., Rotman M., Cassel D. The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex localization. Science. 270:1995;1999-2002.
    • (1995) Science , vol.270 , pp. 1999-2002
    • Cukierman, E.1    Huber, I.2    Rotman, M.3    Cassel, D.4
  • 66
    • 0034767944 scopus 로고    scopus 로고
    • Yeast Rab GTPase-activating protein Gyp1p localizes to the Golgi apparatus and is a negative regulator of Ypt1p
    • Du L.L., Novick P. Yeast Rab GTPase-activating protein Gyp1p localizes to the Golgi apparatus and is a negative regulator of Ypt1p. Mol Biol Cell. 12:2001;1215-1226.
    • (2001) Mol Biol Cell , vol.12 , pp. 1215-1226
    • Du, L.L.1    Novick, P.2
  • 67
    • 0035899863 scopus 로고    scopus 로고
    • Characterization of MTMR3. an inositol lipid 3-phosphatase with novel substrate specificity
    • Walker D.M., Urbe S., Dove S.K., Tenza D., Raposo G., Clague M.J. Characterization of MTMR3. an inositol lipid 3-phosphatase with novel substrate specificity. Curr Biol. 11:2001;1600-1605.
    • (2001) Curr Biol , vol.11 , pp. 1600-1605
    • Walker, D.M.1    Urbe, S.2    Dove, S.K.3    Tenza, D.4    Raposo, G.5    Clague, M.J.6
  • 68
    • 0035853708 scopus 로고    scopus 로고
    • Biochemical characterization of Gyp6p, a Ypt/Rab-specific GTPase-activating protein from yeast
    • Will E., Gallwitz D. Biochemical characterization of Gyp6p, a Ypt/Rab-specific GTPase-activating protein from yeast. J Biol Chem. 276:2001;12135-12139.
    • (2001) J Biol Chem , vol.276 , pp. 12135-12139
    • Will, E.1    Gallwitz, D.2
  • 70
    • 0034946168 scopus 로고    scopus 로고
    • The mammalian guanine nucleotide exchange factor mSec12 is essential for activation of the Sar1 GTPase directing endoplasmic reticulum export
    • Weissman J.T., Plutner H., Balch W.E. The mammalian guanine nucleotide exchange factor mSec12 is essential for activation of the Sar1 GTPase directing endoplasmic reticulum export. Traffic. 2:2001;465-475.
    • (2001) Traffic , vol.2 , pp. 465-475
    • Weissman, J.T.1    Plutner, H.2    Balch, W.E.3
  • 71
    • 0035809932 scopus 로고    scopus 로고
    • Rer1p, a retrieval receptor for endoplasmic reticulum membrane proteins, is dynamically localized to the Golgi apparatus by coatomer
    • Sato K., Sato M., Nakano A. Rer1p, a retrieval receptor for endoplasmic reticulum membrane proteins, is dynamically localized to the Golgi apparatus by coatomer. J Cell Biol. 152:2001;935-944.
    • (2001) J Cell Biol , vol.152 , pp. 935-944
    • Sato, K.1    Sato, M.2    Nakano, A.3
  • 72
    • 0035661564 scopus 로고    scopus 로고
    • Golgi-to-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsl1p, a component of the ER target site that interacts with a COPI coat subunit
    • Reilly B.A., Kraynack B.A., VanRheenen S.M., Waters M.G. Golgi-to-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsl1p, a component of the ER target site that interacts with a COPI coat subunit. Mol Biol Cell. 12:2001;3783-3796. This paper describes a protein complex of the ER that is a good candidate to be responsible for tethering Golgi-derived retrograde vesicles. It contains at least Dsl1p, Sec20p and Tip20p, and there are homologous proteins in the genomes of higher eukaryotes.
    • (2001) Mol Biol Cell , vol.12 , pp. 3783-3796
    • Reilly, B.A.1    Kraynack, B.A.2    VanRheenen, S.M.3    Waters, M.G.4
  • 73
    • 0035914416 scopus 로고    scopus 로고
    • The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast
    • Andag U., Neumann T., Schmitt H.D. The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast. J Biol Chem. 276:2001;39150-39160.
    • (2001) J Biol Chem , vol.276 , pp. 39150-39160
    • Andag, U.1    Neumann, T.2    Schmitt, H.D.3
  • 74
    • 0034602319 scopus 로고    scopus 로고
    • Functional characterization of a mammalian Sac1 and mutants exhibiting substrate-specific defects in phosphoinositide phosphatase activity
    • Nemoto Y., Kearns B.G., Wenk M.R., Chen H., Mori K., Alb J.G. Jr., De Camilli P., Bankaitis V.A. Functional characterization of a mammalian Sac1 and mutants exhibiting substrate-specific defects in phosphoinositide phosphatase activity. J Biol Chem. 275:2000;34293-34305.
    • (2000) J Biol Chem , vol.275 , pp. 34293-34305
    • Nemoto, Y.1    Kearns, B.G.2    Wenk, M.R.3    Chen, H.4    Mori, K.5    Alb J.G., Jr.6    De Camilli, P.7    Bankaitis, V.A.8
  • 75
    • 0037017395 scopus 로고    scopus 로고
    • Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells
    • Barbero P., Bittova L., Pfeffer S.R. Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells. J Cell Biol. 156:2002;511-518.
    • (2002) J Cell Biol , vol.156 , pp. 511-518
    • Barbero, P.1    Bittova, L.2    Pfeffer, S.R.3
  • 76
    • 0031048762 scopus 로고    scopus 로고
    • Rab7: NMR and kinetics analysis of intact and C-terminal truncated constructs
    • Neu M., Brachvogel V., Oschkinat H., Zerial M., Metcalf P. Rab7: NMR and kinetics analysis of intact and C-terminal truncated constructs. Proteins. 27:1997;204-209.
    • (1997) Proteins , vol.27 , pp. 204-209
    • Neu, M.1    Brachvogel, V.2    Oschkinat, H.3    Zerial, M.4    Metcalf, P.5
  • 77
    • 0033638091 scopus 로고    scopus 로고
    • The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32
    • Jones S., Newman C., Liu F., Segev N. The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32. Mol Biol Cell. 11:2000;4403-4411.
    • (2000) Mol Biol Cell , vol.11 , pp. 4403-4411
    • Jones, S.1    Newman, C.2    Liu, F.3    Segev, N.4
  • 78
    • 0034676094 scopus 로고    scopus 로고
    • TRAPP stimulates guanine nucleotide exchange on Ypt1p
    • Wang W., Sacher M., Ferro-Novick S. TRAPP stimulates guanine nucleotide exchange on Ypt1p. J Cell Biol. 151:2000;289-296.
    • (2000) J Cell Biol , vol.151 , pp. 289-296
    • Wang, W.1    Sacher, M.2    Ferro-Novick, S.3
  • 81
    • 0034599839 scopus 로고    scopus 로고
    • The role of the COOH terminus of Sec2p in the transport of post-Golgi vesicles
    • Elkind N.B., Walch-Solimena C., Novick P.J. The role of the COOH terminus of Sec2p in the transport of post-Golgi vesicles. J Cell Biol. 149:2000;95-110.
    • (2000) J Cell Biol , vol.149 , pp. 95-110
    • Elkind, N.B.1    Walch-Solimena, C.2    Novick, P.J.3
  • 82
    • 0037155216 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate-interacting domains in PIKfyve. Binding specificity and role in PIKfyve endomembrane localization
    • Sbrissa D., Ikonomov O.C., Shisheva A. Phosphatidylinositol 3-phosphate-interacting domains in PIKfyve. Binding specificity and role in PIKfyve endomembrane localization. J Biol Chem. 277:2002;6073-6079.
    • (2002) J Biol Chem , vol.277 , pp. 6073-6079
    • Sbrissa, D.1    Ikonomov, O.C.2    Shisheva, A.3
  • 83
    • 0037128929 scopus 로고    scopus 로고
    • Osmotic stress-induced increase of phosphatidylinositol 3,5-bisphosphate requires Vac14p, an activator of the lipid kinase Fab1p
    • Bonangelino C.J., Nau J.J., Duex J.E., Brinkman M., Wurmser A.E., Gary J.D., Emr S.D., Weisman L.S. Osmotic stress-induced increase of phosphatidylinositol 3,5-bisphosphate requires Vac14p, an activator of the lipid kinase Fab1p. J Cell Biol. 156:2002;1015-1028. Both yeast and mammalian cells have a lipid kinase that generates phosphatidylinositol 3,5-bisphosphate, and in yeast this lipid is induced by osmotic stress. So far, no proteins or domains that recognise phosphatidylinositol 3,5-bisphosphate have been identified, but this paper provides good evidence that the lipid controls the size and morphology of the vacuole. The activity, but not the membrane binding, of the kinase is dependent on the proteins Vac7p [84] and Vac14p, with the latter having homologues in higher eukaryotes.
    • (2002) J Cell Biol , vol.156 , pp. 1015-1028
    • Bonangelino, C.J.1    Nau, J.J.2    Duex, J.E.3    Brinkman, M.4    Wurmser, A.E.5    Gary, J.D.6    Emr, S.D.7    Weisman, L.S.8
  • 84
    • 0036231465 scopus 로고    scopus 로고
    • Regulation of Fab1 phosphatidylinositol 3-phosphate 5-kinase pathway by Vac7 protein and Fig4, a polyphosphoinositide phosphatase family member
    • Gary J.D., Sato T.K., Stefan C.J., Bonangelino C.J., Weisman L.S., Emr S.D. Regulation of Fab1 phosphatidylinositol 3-phosphate 5-kinase pathway by Vac7 protein and Fig4, a polyphosphoinositide phosphatase family member. Mol Biol Cell. 13:2002;1238-1251.
    • (2002) Mol Biol Cell , vol.13 , pp. 1238-1251
    • Gary, J.D.1    Sato, T.K.2    Stefan, C.J.3    Bonangelino, C.J.4    Weisman, L.S.5    Emr, S.D.6


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