메뉴 건너뛰기




Volumn 17, Issue 4, 2005, Pages 402-408

The Fab1 phosphatidylinositol kinase pathway in the regulation of vacuole morphology

Author keywords

[No Author keywords available]

Indexed keywords

LIPID; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL KINASE; PHOSPHOTRANSFERASE;

EID: 22044457181     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2005.06.002     Document Type: Review
Times cited : (81)

References (47)
  • 1
    • 0031911736 scopus 로고    scopus 로고
    • Vacuole biogenesis in Saccharomyces cerevisiae: Protein transport pathways to the yeast vacuole
    • N.J. Bryant, and T.H. Stevens Vacuole biogenesis in Saccharomyces cerevisiae: protein transport pathways to the yeast vacuole Microbiol Mol Biol Rev 62 1998 230 247
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 230-247
    • Bryant, N.J.1    Stevens, T.H.2
  • 2
    • 0347416707 scopus 로고    scopus 로고
    • Yeast vacuole inheritance and dynamics
    • L.S. Weisman Yeast vacuole inheritance and dynamics Annu Rev Genet 37 2003 435 460
    • (2003) Annu Rev Genet , vol.37 , pp. 435-460
    • Weisman, L.S.1
  • 3
    • 0032217266 scopus 로고    scopus 로고
    • Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body
    • G. Odorizzi, M. Babst, and S.D. Emr Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body Cell 95 1998 847 858
    • (1998) Cell , vol.95 , pp. 847-858
    • Odorizzi, G.1    Babst, M.2    Emr, S.D.3
  • 4
    • 0031854866 scopus 로고    scopus 로고
    • Retrograde traffic out of the yeast vacuole to the TGN occurs via the prevacuolar/endosomal compartment
    • N.J. Bryant, R.C. Piper, L.S. Weisman, and T.H. Stevens Retrograde traffic out of the yeast vacuole to the TGN occurs via the prevacuolar/endosomal compartment J Cell Biol 142 1998 651 663
    • (1998) J Cell Biol , vol.142 , pp. 651-663
    • Bryant, N.J.1    Piper, R.C.2    Weisman, L.S.3    Stevens, T.H.4
  • 5
    • 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
    • A.E. Wurmser, T.K. Sato, and S.D. Emr 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
  • 6
    • 0028788311 scopus 로고
    • The GTPase Ypt7p of Saccharomyces cerevisiae is required on both partner vacuoles for the homotypic fusion step of vacuole inheritance
    • A. Haas, D. Scheglmann, T. Lazar, D. Gallwitz, and W. Wickner The GTPase Ypt7p of Saccharomyces cerevisiae is required on both partner vacuoles for the homotypic fusion step of vacuole inheritance EMBO J 14 1995 5258 5270
    • (1995) EMBO J , vol.14 , pp. 5258-5270
    • Haas, A.1    Scheglmann, D.2    Lazar, T.3    Gallwitz, D.4    Wickner, W.5
  • 7
    • 0034943323 scopus 로고    scopus 로고
    • The class C Vps complex functions at multiple stages of the vacuolar transport pathway
    • M.R. Peterson, and S.D. Emr The class C Vps complex functions at multiple stages of the vacuolar transport pathway Traffic 2 2001 476 486
    • (2001) Traffic , vol.2 , pp. 476-486
    • Peterson, M.R.1    Emr, S.D.2
  • 8
    • 0033634646 scopus 로고    scopus 로고
    • Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion
    • T.K. Sato, P. Rehling, M.R. Peterson, and S.D. Emr Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion Mol Cell 6 2000 661 671
    • (2000) Mol Cell , vol.6 , pp. 661-671
    • Sato, T.K.1    Rehling, P.2    Peterson, M.R.3    Emr, S.D.4
  • 9
  • 10
    • 11144240474 scopus 로고    scopus 로고
    • Diacylglycerol and its formation by phospholipase C regulate Rab- and SNARE-dependent yeast vacuole fusion
    • Y. Jun, R.A. Fratti, and W. Wickner Diacylglycerol and its formation by phospholipase C regulate Rab- and SNARE-dependent yeast vacuole fusion J Biol Chem 279 2004 53186 53195
    • (2004) J Biol Chem , vol.279 , pp. 53186-53195
    • Jun, Y.1    Fratti, R.A.2    Wickner, W.3
  • 11
    • 11244258475 scopus 로고    scopus 로고
    • Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles
    • R.A. Fratti, Y. Jun, A.J. Merz, N. Margolis, and W. Wickner Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles J Cell Biol 167 2004 1087 1098
    • (2004) J Cell Biol , vol.167 , pp. 1087-1098
    • Fratti, R.A.1    Jun, Y.2    Merz, A.J.3    Margolis, N.4    Wickner, W.5
  • 12
    • 0037086618 scopus 로고    scopus 로고
    • Yeast vacuoles and membrane fusion pathways
    • W. Wickner Yeast vacuoles and membrane fusion pathways EMBO J 21 2002 1241 1247
    • (2002) EMBO J , vol.21 , pp. 1241-1247
    • Wickner, W.1
  • 13
    • 13944275304 scopus 로고    scopus 로고
    • Expanding dynamin: From fission to fusion
    • K. Peplowska, and C. Ungermann Expanding dynamin: from fission to fusion Nat Cell Biol 7 2005 103 104
    • (2005) Nat Cell Biol , vol.7 , pp. 103-104
    • Peplowska, K.1    Ungermann, C.2
  • 14
    • 0035854730 scopus 로고    scopus 로고
    • Mammalian cell morphology and endocytic membrane homeostasis require enzymatically active phosphoinositide 5-kinase PIKfyve
    • O.C. Ikonomov, D. Sbrissa, and A. Shisheva Mammalian cell morphology and endocytic membrane homeostasis require enzymatically active phosphoinositide 5-kinase PIKfyve J Biol Chem 276 2001 26141 26147
    • (2001) J Biol Chem , vol.276 , pp. 26141-26147
    • Ikonomov, O.C.1    Sbrissa, D.2    Shisheva, A.3
  • 15
    • 0032487577 scopus 로고    scopus 로고
    • Fab1p is essential for PtdIns(3)P 5-kinase activity and the maintenance of vacuolar size and membrane homeostasis
    • J.D. Gary, A.E. Wurmser, C.J. Bonangelino, L.S. Weisman, and S.D. Emr Fab1p is essential for PtdIns(3)P 5-kinase activity and the maintenance of vacuolar size and membrane homeostasis J Cell Biol 143 1998 65 79
    • (1998) J Cell Biol , vol.143 , pp. 65-79
    • Gary, J.D.1    Wurmser, A.E.2    Bonangelino, C.J.3    Weisman, L.S.4    Emr, S.D.5
  • 16
    • 0032488032 scopus 로고    scopus 로고
    • The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p is essential for vacuole function in S. cerevisiae
    • F.T. Cooke, S.K. Dove, R.K. McEwen, G. Painter, A.B. Holmes, M.N. Hall, R.H. Michell, and P.J. Parker The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p is essential for vacuole function in S. cerevisiae Curr Biol 8 1998 1219 1222
    • (1998) Curr Biol , vol.8 , pp. 1219-1222
    • Cooke, F.T.1    Dove, S.K.2    McEwen, R.K.3    Painter, G.4    Holmes, A.B.5    Hall, M.N.6    Michell, R.H.7    Parker, P.J.8
  • 17
    • 0346729925 scopus 로고    scopus 로고
    • Vacuole size control: Regulation of PtdIns(3,5)P2 levels by the vacuole-associated Vac14-Fig4 complex, a PtdIns(35)P2-specific phosphatase
    • 2 5-phosphatase in vitro. Intriguingly, localization of Fig4p to the vacuole membrane is dependent on a physical interaction with Vac14p. Thus, paradoxically, Vac14p not only functions as an activator of Fab1p, but also recruits the phosphatase that counters its PtdIns3P 5-kinase kinase activity. The authors propose that fluctuations in the relative stoichiometry of Fig4p and Vac14p across the vacuolar membrane might give rise to microdomains that would favor one reaction of the other (i.e. phosphorylation by Fab1p versus dephosphorylation by Fig4p).
    • (2004) Mol Biol Cell , vol.15 , pp. 24-36
    • Rudge, S.A.1    Anderson, D.M.2    Emr, S.D.3
  • 18
    • 0029024442 scopus 로고
    • Novel PI(4)P 5-kinase homologue, Fab1p, essential for normal vacuole function and morphology in yeast
    • A. Yamamoto, D.B. DeWald, I.V. Boronenkov, R.A. Anderson, S.D. Emr, and D. Koshland Novel PI(4)P 5-kinase homologue, Fab1p, essential for normal vacuole function and morphology in yeast Mol Biol Cell 6 1995 525 539
    • (1995) Mol Biol Cell , vol.6 , pp. 525-539
    • Yamamoto, A.1    Dewald, D.B.2    Boronenkov, I.V.3    Anderson, R.A.4    Emr, S.D.5    Koshland, D.6
  • 19
    • 0037018842 scopus 로고    scopus 로고
    • Vac14 controls PtdIns(3,5)P(2) synthesis and Fab1-dependent protein trafficking to the multivesicular body
    • S.K. Dove, R.K. McEwen, A. Mayes, D.C. Hughes, J.D. Beggs, and R.H. Michell Vac14 controls PtdIns(3,5)P(2) synthesis and Fab1-dependent protein trafficking to the multivesicular body Curr Biol 12 2002 885 893
    • (2002) Curr Biol , vol.12 , pp. 885-893
    • Dove, S.K.1    McEwen, R.K.2    Mayes, A.3    Hughes, D.C.4    Beggs, J.D.5    Michell, R.H.6
  • 20
    • 0030692711 scopus 로고    scopus 로고
    • Vac7p, a novel vacuolar protein, is required for normal vacuole inheritance and morphology
    • C.J. Bonangelino, N.L. Catlett, and L.S. Weisman Vac7p, a novel vacuolar protein, is required for normal vacuole inheritance and morphology Mol Cell Biol 17 1997 6847 6858
    • (1997) Mol Cell Biol , vol.17 , pp. 6847-6858
    • Bonangelino, C.J.1    Catlett, N.L.2    Weisman, L.S.3
  • 21
    • 0036231465 scopus 로고    scopus 로고
    • Regulation of Fab1 phosphatidylinositol 3-phosphate 5-kinase pathway by Vac7 protein and Fig4, a polyphosphoinositide phosphatase family member
    • J.D. Gary, T.K. Sato, C.J. Stefan, C.J. Bonangelino, L.S. Weisman, and S.D. Emr 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
  • 22
    • 0037128929 scopus 로고    scopus 로고
    • Osmotic stress-induced increase of phosphatidylinositol 3,5-bisphosphate requires Vac14p, an activator of the lipid kinase Fab1p
    • C.J. Bonangelino, J.J. Nau, J.E. Duex, M. Brinkman, A.E. Wurmser, J.D. Gary, S.D. Emr, and L.S. Weisman 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
    • (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
  • 23
    • 1342325811 scopus 로고    scopus 로고
    • Isolation of suppressor mutants of phosphatidylinositol 3-phosphate 5-kinase deficient cells in Schizosaccharomyces pombe
    • M. Onishi, Y. Nakamura, T. Koga, K. Takegawa, and Y. Fukui Isolation of suppressor mutants of phosphatidylinositol 3-phosphate 5-kinase deficient cells in Schizosaccharomyces pombe Biosci Biotechnol Biochem 67 2003 1772 1779
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 1772-1779
    • Onishi, M.1    Nakamura, Y.2    Koga, T.3    Takegawa, K.4    Fukui, Y.5
  • 24
    • 0035808040 scopus 로고    scopus 로고
    • The complex and intriguing lives of PIP2 with ion channels and transporters
    • D.W. Hilgemann, S. Feng, and C. Nasuhoglu The complex and intriguing lives of PIP2 with ion channels and transporters Sci STKE 2001 2001 RE19
    • (2001) Sci STKE , vol.2001 , pp. 19
    • Hilgemann, D.W.1    Feng, S.2    Nasuhoglu, C.3
  • 25
    • 3142583199 scopus 로고    scopus 로고
    • Svp1p defines a family of phosphatidylinositol 3,5-bisphosphate effectors
    • 2 in vitro and localizes to the vacuolar membrane in a Fab1p-dependent fashion. The lipid interaction motif was mapped within one of seven WD-40 motifs comprising a β-propeller fold. Thus, Atg18p, along with its homologs Atg21p and Ygr223cp, defines a new family of phosphoinositide-binding proteins. Based on results obtained using the RS-ALP recycling assay, the authors proposed that Atg18p modulates membrane retrieval from the vacuole as an effector of Fab1p.
    • (2004) EMBO J , vol.23 , pp. 1922-1933
    • Dove, S.K.1    Piper, R.C.2    McEwen, R.K.3    Yu, J.W.4    King, M.C.5    Hughes, D.C.6    Thuring, J.7    Holmes, A.B.8    Cooke, F.T.9    Michell, R.H.10
  • 26
    • 0346503885 scopus 로고    scopus 로고
    • The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure
    • F. Reggiori, K.A. Tucker, P.E. Stromhaug, and D.J. Klionsky The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure Dev Cell 6 2004 79 90
    • (2004) Dev Cell , vol.6 , pp. 79-90
    • Reggiori, F.1    Tucker, K.A.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 27
    • 13444251066 scopus 로고    scopus 로고
    • The vacuolar kinase Yck3 maintains organelle fragmentation by regulating the HOPS tethering complex
    • T.J. Lagrassa, and C. Ungermann The vacuolar kinase Yck3 maintains organelle fragmentation by regulating the HOPS tethering complex J Cell Biol 168 2005 401 414 This study aims to identify factors required for maintenance of fragmented vacuoles under hypertonic shock. One of the proteins identified is the vacuolar casein kinase I Yck3p, which appears to prevent rapid fusion of fragmented vacuoles by phosphorylating the Class C Vps/HOPS complex component Vps41p. The authors suggest that phosphorylation of tethering complexes might be a more general mechanism for regulation of membrane dynamics.
    • (2005) J Cell Biol , vol.168 , pp. 401-414
    • Lagrassa, T.J.1    Ungermann, C.2
  • 28
    • 8844281541 scopus 로고    scopus 로고
    • Mutual control of membrane fission and fusion proteins
    • C. Peters, T.L. Baars, S. Buhler, and A. Mayer Mutual control of membrane fission and fusion proteins Cell 119 2004 667 678 This work is the first to propose a mutual and reciprocal regulation of the fusion and fission machineries. The authors demonstrate that Vps1p, a yeast dynamin homolog, polymerizes onto vacuolar t-SNAREs, an event suggested to preclude futile formation of cis-SNARE complexes. At the onset of fusion, independently of α-SNAP and v-SNAREs, NSF/Sec18 and t-SNAREs induce depolymerization of Vps1p to liberate the t-SNAREs. Disassembly of Vps1 polymers by the fusion machinery is also proposed to regulate membrane scission.
    • (2004) Cell , vol.119 , pp. 667-678
    • Peters, C.1    Baars, T.L.2    Buhler, S.3    Mayer, A.4
  • 29
    • 0024095176 scopus 로고
    • Organelle assembly in yeast: Characterization of yeast mutants defective in vacuolar biogenesis and protein sorting
    • L.M. Banta, J.S. Robinson, D.J. Klionsky, and S.D. Emr Organelle assembly in yeast: characterization of yeast mutants defective in vacuolar biogenesis and protein sorting J Cell Biol 107 1988 1369 1383
    • (1988) J Cell Biol , vol.107 , pp. 1369-1383
    • Banta, L.M.1    Robinson, J.S.2    Klionsky, D.J.3    Emr, S.D.4
  • 30
    • 1842784049 scopus 로고    scopus 로고
    • The biogenesis of multivesicular endosomes
    • J. Gruenberg, and H. Stenmark The biogenesis of multivesicular endosomes Nat Rev Mol Cell Biol 5 2004 317 323
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 317-323
    • Gruenberg, J.1    Stenmark, H.2
  • 31
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • D.J. Katzmann, G. Odorizzi, and S.D. Emr Receptor downregulation and multivesicular-body sorting Nat Rev Mol Cell Biol 3 2002 893 905
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 32
    • 0742288063 scopus 로고    scopus 로고
    • Multivesicular body sorting: Ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S
    • D.J. Katzmann, S. Sarkar, T. Chu, A. Audhya, and S.D. Emr Multivesicular body sorting: ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S Mol Biol Cell 15 2004 468 480
    • (2004) Mol Biol Cell , vol.15 , pp. 468-480
    • Katzmann, D.J.1    Sarkar, S.2    Chu, T.3    Audhya, A.4    Emr, S.D.5
  • 33
    • 0141532093 scopus 로고    scopus 로고
    • Identification of mammalian Vps24p as an effector of phosphatidylinositol 3,5-bisphosphate-dependent endosome compartmentalization
    • P. Whitley, B.J. Reaves, M. Hashimoto, A.M. Riley, B.V. Potter, and G.D. Holman Identification of mammalian Vps24p as an effector of phosphatidylinositol 3,5-bisphosphate-dependent endosome compartmentalization J Biol Chem 278 2003 38786 38795
    • (2003) J Biol Chem , vol.278 , pp. 38786-38795
    • Whitley, P.1    Reaves, B.J.2    Hashimoto, M.3    Riley, A.M.4    Potter, B.V.5    Holman, G.D.6
  • 34
    • 3042723253 scopus 로고    scopus 로고
    • Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body
    • A. Eugster, E.I. Pecheur, F. Michel, B. Winsor, F. Letourneur, and S. Friant Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body Mol Biol Cell 15 2004 3031 3041
    • (2004) Mol Biol Cell , vol.15 , pp. 3031-3041
    • Eugster, A.1    Pecheur, E.I.2    Michel, F.3    Winsor, B.4    Letourneur, F.5    Friant, S.6
  • 36
    • 0037088590 scopus 로고    scopus 로고
    • Functional dissection of lipid and protein kinase signals of PIKfyve reveals the role of PtdIns 3,5-P2 production for endomembrane integrity
    • O.C. Ikonomov, D. Sbrissa, K. Mlak, M. Kanzaki, J. Pessin, and A. Shisheva Functional dissection of lipid and protein kinase signals of PIKfyve reveals the role of PtdIns 3,5-P2 production for endomembrane integrity J Biol Chem 277 2002 9206 9211
    • (2002) J Biol Chem , vol.277 , pp. 9206-9211
    • Ikonomov, O.C.1    Sbrissa, D.2    Mlak, K.3    Kanzaki, M.4    Pessin, J.5    Shisheva, A.6
  • 37
    • 0034735536 scopus 로고    scopus 로고
    • Autophagic tubes: Vacuolar invaginations involved in lateral membrane sorting and inverse vesicle budding
    • O. Muller, T. Sattler, M. Flotenmeyer, H. Schwarz, H. Plattner, and A. Mayer Autophagic tubes: vacuolar invaginations involved in lateral membrane sorting and inverse vesicle budding J Cell Biol 151 2000 519 528
    • (2000) J Cell Biol , vol.151 , pp. 519-528
    • Muller, O.1    Sattler, T.2    Flotenmeyer, M.3    Schwarz, H.4    Plattner, H.5    Mayer, A.6
  • 38
    • 2342476913 scopus 로고    scopus 로고
    • The osmotic stress response of Saccharomyces cerevisiae
    • M.J. Tamas, and S. Hohmann The osmotic stress response of Saccharomyces cerevisiae Topics in Current Genetics 1 2003 121 200
    • (2003) Topics in Current Genetics , vol.1 , pp. 121-200
    • Tamas, M.J.1    Hohmann, S.2
  • 39
    • 4043098376 scopus 로고    scopus 로고
    • MAP kinase-mediated stress relief that precedes and regulates the timing of transcriptional induction
    • M. Proft, and K. Struhl MAP kinase-mediated stress relief that precedes and regulates the timing of transcriptional induction Cell 118 2004 351 361
    • (2004) Cell , vol.118 , pp. 351-361
    • Proft, M.1    Struhl, K.2
  • 40
    • 0027261550 scopus 로고
    • Evidence for a dual osmoregulatory mechanism in the yeast Saccharomyces cerevisiae
    • M. Latterich, and M.D. Watson Evidence for a dual osmoregulatory mechanism in the yeast Saccharomyces cerevisiae Biochem Biophys Res Commun 191 1993 1111 1117
    • (1993) Biochem Biophys Res Commun , vol.191 , pp. 1111-1117
    • Latterich, M.1    Watson, M.D.2
  • 41
    • 0032426664 scopus 로고    scopus 로고
    • The terminal tail region of a yeast myosin-V mediates its attachment to vacuole membranes and sites of polarized growth
    • N.L. Catlett, and L.S. Weisman The terminal tail region of a yeast myosin-V mediates its attachment to vacuole membranes and sites of polarized growth Proc Natl Acad Sci USA 95 1998 14799 14804
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14799-14804
    • Catlett, N.L.1    Weisman, L.S.2
  • 42
    • 0025952205 scopus 로고
    • Vacuolar segregation to the bud of Saccharomyces cerevisiae: An analysis of morphology and timing in the cell cycle
    • D.S. Gomes de Mesquita, R. ten Hoopen, and C.L. Woldringh Vacuolar segregation to the bud of Saccharomyces cerevisiae: an analysis of morphology and timing in the cell cycle J Gen Microbiol 137 1991 2447 2454
    • (1991) J Gen Microbiol , vol.137 , pp. 2447-2454
    • Gomes De Mesquita, D.S.1    Ten Hoopen, R.2    Woldringh, C.L.3
  • 43
    • 0037422115 scopus 로고    scopus 로고
    • Regulated degradation of a class V myosin receptor directs movement of the yeast vacuole
    • F. Tang, E.J. Kauffman, J.L. Novak, J.J. Nau, N.L. Catlett, and L.S. Weisman Regulated degradation of a class V myosin receptor directs movement of the yeast vacuole Nature 422 2003 87 92
    • (2003) Nature , vol.422 , pp. 87-92
    • Tang, F.1    Kauffman, E.J.2    Novak, J.L.3    Nau, J.J.4    Catlett, N.L.5    Weisman, L.S.6
  • 44
    • 0242286618 scopus 로고    scopus 로고
    • The G1 cyclin Cln3p controls vacuolar biogenesis in Saccharomyces cerevisiae
    • B.K. Han, R. Aramayo, and M. Polymenis The G1 cyclin Cln3p controls vacuolar biogenesis in Saccharomyces cerevisiae Genetics 165 2003 467 476
    • (2003) Genetics , vol.165 , pp. 467-476
    • Han, B.K.1    Aramayo, R.2    Polymenis, M.3
  • 45
    • 0030816513 scopus 로고    scopus 로고
    • Vacuole segregation in the Saccharomyces cerevisiae vac2-1 mutant: Structural and biochemical quantification of the segregation defect and formation of new vacuoles
    • D.S. Gomes De Mesquita, J. Shaw, J.A. Grimbergen, M.A. Buys, L. Dewi, and C.L. Woldringh Vacuole segregation in the Saccharomyces cerevisiae vac2-1 mutant: structural and biochemical quantification of the segregation defect and formation of new vacuoles Yeast 13 1997 999 1008
    • (1997) Yeast , vol.13 , pp. 999-1008
    • Gomes De Mesquita, D.S.1    Shaw, J.2    Grimbergen, J.A.3    Buys, M.A.4    Dewi, L.5    Woldringh, C.L.6
  • 46
    • 14844328642 scopus 로고    scopus 로고
    • Acquisition of unprecedented phosphatidylinositol 3,5-Bisphosphate rise in hyperosmotically stressed 3T3-L1 adipocytes, mediated by ArPIKfyve-PIKfyve pathway
    • D. Sbrissa, and A. Shisheva Acquisition of unprecedented phosphatidylinositol 3,5-Bisphosphate rise in hyperosmotically stressed 3T3-L1 adipocytes, mediated by ArPIKfyve-PIKfyve pathway J Biol Chem 280 2005 7883 7889
    • (2005) J Biol Chem , vol.280 , pp. 7883-7889
    • Sbrissa, D.1    Shisheva, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.