메뉴 건너뛰기




Volumn 7, Issue 7, 2012, Pages

Involvement of the Penta-EF-hand protein Pef1p in the Ca2+-dependent regulation of COPII subunit assembly in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; CALCIUM ION; COAT PROTEIN COMPLEX II; COAT PROTEIN COMPLEX II SEC13 SUBUNIT; COAT PROTEIN COMPLEX II SEC31A SUBUNIT; COAT PROTEIN COMPLEX II SEC31P SUBUNIT; PROTEIN ALG 2; PROTEIN PEF1P; UNCLASSIFIED DRUG;

EID: 84863811537     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0040765     Document Type: Article
Times cited : (12)

References (42)
  • 1
    • 77953642000 scopus 로고    scopus 로고
    • Protein sorting receptors in the early secretory pathway
    • Dancourt J, Barlowe C, (2010) Protein sorting receptors in the early secretory pathway. Annu Rev Biochem 79: 777-802.
    • (2010) Annu Rev Biochem , vol.79 , pp. 777-802
    • Dancourt, J.1    Barlowe, C.2
  • 3
    • 0027500969 scopus 로고
    • SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER
    • Barlowe C, Schekman R, (1993) SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER. Nature 365: 347-349.
    • (1993) Nature , vol.365 , pp. 347-349
    • Barlowe, C.1    Schekman, R.2
  • 4
    • 0035842886 scopus 로고    scopus 로고
    • Crystal structure of Sar1-GDP at 1.7 A resolution and the role of the NH2 terminus in ER export
    • Huang M, Weissman JT, Beraud-Dufour S, Luan P, Wang C, et al. (2001) Crystal structure of Sar1-GDP at 1.7 A resolution and the role of the NH2 terminus in ER export. J Cell Biol 155: 937-948.
    • (2001) J Cell Biol , vol.155 , pp. 937-948
    • Huang, M.1    Weissman, J.T.2    Beraud-Dufour, S.3    Luan, P.4    Wang, C.5
  • 5
    • 0037136560 scopus 로고    scopus 로고
    • Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat
    • Bi X, Corpina RA, Goldberg J, (2002) Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat. Nature 419: 271-277.
    • (2002) Nature , vol.419 , pp. 271-277
    • Bi, X.1    Corpina, R.A.2    Goldberg, J.3
  • 6
    • 0043029286 scopus 로고    scopus 로고
    • SNARE selectivity of the COPII coat
    • Mossessova E, Bickford LC, Goldberg J, (2003) SNARE selectivity of the COPII coat. Cell 114: 483-495.
    • (2003) Cell , vol.114 , pp. 483-495
    • Mossessova, E.1    Bickford, L.C.2    Goldberg, J.3
  • 7
    • 0041526467 scopus 로고    scopus 로고
    • Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles
    • Miller EA, Beilharz TH, Malkus PN, Lee MC, Hamamoto S, et al. (2003) Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114: 497-509.
    • (2003) Cell , vol.114 , pp. 497-509
    • Miller, E.A.1    Beilharz, T.H.2    Malkus, P.N.3    Lee, M.C.4    Hamamoto, S.5
  • 8
    • 0032495477 scopus 로고    scopus 로고
    • COPII-cargo interactions direct protein sorting into ER-derived transport vesicles
    • Kuehn MJ, Herrmann JM, Schekman R, (1998) COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature 391: 187-190.
    • (1998) Nature , vol.391 , pp. 187-190
    • Kuehn, M.J.1    Herrmann, J.M.2    Schekman, R.3
  • 9
    • 0027467609 scopus 로고
    • Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum
    • Yoshihisa T, Barlowe C, Schekman R, (1993) Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum. Science 259: 1466-1468.
    • (1993) Science , vol.259 , pp. 1466-1468
    • Yoshihisa, T.1    Barlowe, C.2    Schekman, R.3
  • 11
    • 15544367075 scopus 로고    scopus 로고
    • Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis
    • Sato K, Nakano A, (2005) Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis. Nat Struct Mol Biol 12: 167-174.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 167-174
    • Sato, K.1    Nakano, A.2
  • 12
    • 9144229521 scopus 로고    scopus 로고
    • GTP/GDP exchange by Sec12p enables COPII vesicle bud formation on synthetic liposomes
    • Futai E, Hamamoto S, Orci L, Schekman R, (2004) GTP/GDP exchange by Sec12p enables COPII vesicle bud formation on synthetic liposomes. EMBO J 23: 4146-4155.
    • (2004) EMBO J , vol.23 , pp. 4146-4155
    • Futai, E.1    Hamamoto, S.2    Orci, L.3    Schekman, R.4
  • 13
    • 70350763840 scopus 로고    scopus 로고
    • Visualization of cargo concentration by COPII minimal machinery in a planar lipid membrane
    • Tabata KV, Sato K, Ide T, Nishizaka T, Nakano A, et al. (2009) Visualization of cargo concentration by COPII minimal machinery in a planar lipid membrane. EMBO J 28: 3279-3289.
    • (2009) EMBO J , vol.28 , pp. 3279-3289
    • Tabata, K.V.1    Sato, K.2    Ide, T.3    Nishizaka, T.4    Nakano, A.5
  • 14
    • 0026046098 scopus 로고
    • Mammalian Sec23p homologue is restricted to the endoplasmic reticulum transitional cytoplasm
    • Orci L, Ravazzola M, Meda P, Holcomb C, Moore HP, et al. (1991) Mammalian Sec23p homologue is restricted to the endoplasmic reticulum transitional cytoplasm. Proc Natl Acad Sci USA 88: 8611-8615.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8611-8615
    • Orci, L.1    Ravazzola, M.2    Meda, P.3    Holcomb, C.4    Moore, H.P.5
  • 15
    • 10144220633 scopus 로고    scopus 로고
    • The organization of endoplasmic reticulum export complexes
    • Bannykh SI, Rowe T, Balch WE, (1996) The organization of endoplasmic reticulum export complexes. J Cell Biol 135: 19-35.
    • (1996) J Cell Biol , vol.135 , pp. 19-35
    • Bannykh, S.I.1    Rowe, T.2    Balch, W.E.3
  • 16
    • 84863830464 scopus 로고    scopus 로고
    • Insights into structural and regulatory roles of Sec16 in COPII vesicle formation at ER exit sites
    • In Press
    • Yorimitsu T, Sato K, (2012) Insights into structural and regulatory roles of Sec16 in COPII vesicle formation at ER exit sites. Mol Biol Cell 23: in press.
    • (2012) Mol Biol Cell , vol.23
    • Yorimitsu, T.1    Sato, K.2
  • 17
    • 0032895860 scopus 로고    scopus 로고
    • Osmotically induced cell volume changes alter anterograde and retrograde transport, Golgi structure, and COPI dissociation
    • Lee TH, Linstedt AD, (1999) Osmotically induced cell volume changes alter anterograde and retrograde transport, Golgi structure, and COPI dissociation. Mol Biol Cell 10: 1445-1462.
    • (1999) Mol Biol Cell , vol.10 , pp. 1445-1462
    • Lee, T.H.1    Linstedt, A.D.2
  • 18
    • 0035158716 scopus 로고    scopus 로고
    • Golgi complex reorganization during muscle differentiation: visualization in living cells and mechanism
    • Lu Z, Joseph D, Bugnard E, Zaal KJ, Ralston E, (2001) Golgi complex reorganization during muscle differentiation: visualization in living cells and mechanism. Mol Biol Cell 12: 795-808.
    • (2001) Mol Biol Cell , vol.12 , pp. 795-808
    • Lu, Z.1    Joseph, D.2    Bugnard, E.3    Zaal, K.J.4    Ralston, E.5
  • 19
    • 0042266395 scopus 로고    scopus 로고
    • Cell-cycle-specific Golgi fragmentation: how and why?
    • Colanzi A, Suetterlin C, Malhotra V, (2003) Cell-cycle-specific Golgi fragmentation: how and why? Curr Opin Cell Biol 15: 462-467.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 462-467
    • Colanzi, A.1    Suetterlin, C.2    Malhotra, V.3
  • 20
    • 1242351264 scopus 로고    scopus 로고
    • Structures, functions and molecular evolution of the penta-EF-hand Ca2+-binding proteins
    • Maki M, Kitaura Y, Satoh H, Ohkouchi S, Shibata H, (2002) Structures, functions and molecular evolution of the penta-EF-hand Ca2+-binding proteins. Biochim Biophys Acta 1600: 51-60.
    • (2002) Biochim Biophys Acta , vol.1600 , pp. 51-60
    • Maki, M.1    Kitaura, Y.2    Satoh, H.3    Ohkouchi, S.4    Shibata, H.5
  • 21
    • 33750534358 scopus 로고    scopus 로고
    • The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A
    • Yamasaki A, Tani K, Yamamoto A, Kitamura N, Komada M, (2006) The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A. Mol Biol Cell 17: 4876-4887.
    • (2006) Mol Biol Cell , vol.17 , pp. 4876-4887
    • Yamasaki, A.1    Tani, K.2    Yamamoto, A.3    Kitamura, N.4    Komada, M.5
  • 22
    • 77949450563 scopus 로고    scopus 로고
    • Vesicular calcium regulates coat retention, fusogenicity, and size of pre-Golgi intermediates
    • Bentley M, Nycz DC, Joglekar A, Fertschai I, Malli R, et al. (2010) Vesicular calcium regulates coat retention, fusogenicity, and size of pre-Golgi intermediates. Mol Biol Cell 21: 1033-1046.
    • (2010) Mol Biol Cell , vol.21 , pp. 1033-1046
    • Bentley, M.1    Nycz, D.C.2    Joglekar, A.3    Fertschai, I.4    Malli, R.5
  • 23
    • 34250745253 scopus 로고    scopus 로고
    • Structure and organization of coat proteins in the COPII cage
    • Fath S, Mancias JD, Bi X, Goldberg J, (2007) Structure and organization of coat proteins in the COPII cage. Cell 129: 1325-1336.
    • (2007) Cell , vol.129 , pp. 1325-1336
    • Fath, S.1    Mancias, J.D.2    Bi, X.3    Goldberg, J.4
  • 24
    • 35549004893 scopus 로고    scopus 로고
    • Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31
    • Bi X, Mancias JD, Goldberg J, (2007) Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31. Dev Cell 13: 635-645.
    • (2007) Dev Cell , vol.13 , pp. 635-645
    • Bi, X.1    Mancias, J.D.2    Goldberg, J.3
  • 25
    • 34547663702 scopus 로고    scopus 로고
    • The yeast penta-EF protein Pef1p is involved in cation-dependent budding and cell polarization
    • Vernarecci S, Colotti G, Ornaghi P, Schiebel E, Chiancone E, et al. (2007) The yeast penta-EF protein Pef1p is involved in cation-dependent budding and cell polarization. Mol Microbiol 65: 1122-1138.
    • (2007) Mol Microbiol , vol.65 , pp. 1122-1138
    • Vernarecci, S.1    Colotti, G.2    Ornaghi, P.3    Schiebel, E.4    Chiancone, E.5
  • 26
    • 0035900480 scopus 로고    scopus 로고
    • Role of Erv29p in Collecting Soluble Secretory Proteins into ER-Derived Transport Vesicles
    • Belden WJ, Barlowe C, (2001) Role of Erv29p in Collecting Soluble Secretory Proteins into ER-Derived Transport Vesicles. Science 294: 1528-1531.
    • (2001) Science , vol.294 , pp. 1528-1531
    • Belden, W.J.1    Barlowe, C.2
  • 28
    • 77951710195 scopus 로고    scopus 로고
    • Requirements for transitional endoplasmic reticulum site structure and function in Saccharomyces cerevisiae
    • Shindiapina P, Barlowe C, (2010) Requirements for transitional endoplasmic reticulum site structure and function in Saccharomyces cerevisiae. Mol Biol Cell 21: 1530-1545.
    • (2010) Mol Biol Cell , vol.21 , pp. 1530-1545
    • Shindiapina, P.1    Barlowe, C.2
  • 29
    • 84863984706 scopus 로고    scopus 로고
    • High-curvature domains of the ER are important for the organization of ER exit sites in Saccharomyces cerevisiae
    • Okamoto M, Kurokawa K, Matsuura-Tokita K, Saito C, Hirata R, et al. (2012) High-curvature domains of the ER are important for the organization of ER exit sites in Saccharomyces cerevisiae. J Cell Sci: in press.
    • (2012) J Cell Sci: In Press
    • Okamoto, M.1    Kurokawa, K.2    Matsuura-Tokita, K.3    Saito, C.4    Hirata, R.5
  • 30
    • 0033043513 scopus 로고    scopus 로고
    • Alix, a novel mouse protein undergoing calcium-dependent interaction with the apoptosis-linked-gene 2 (ALG-2) protein
    • Missotten M, Nichols A, Rieger K, Sadoul R, (1999) Alix, a novel mouse protein undergoing calcium-dependent interaction with the apoptosis-linked-gene 2 (ALG-2) protein. Cell Death Differ 6: 124-129.
    • (1999) Cell Death Differ , vol.6 , pp. 124-129
    • Missotten, M.1    Nichols, A.2    Rieger, K.3    Sadoul, R.4
  • 31
    • 0033556043 scopus 로고    scopus 로고
    • Cloning of AIP1, a novel protein that associates with the apoptosis-linked gene ALG-2 in a Ca2+-dependent reaction
    • Vito P, Pellegrini L, Guiet C, D'Adamio L, (1999) Cloning of AIP1, a novel protein that associates with the apoptosis-linked gene ALG-2 in a Ca2+-dependent reaction. J Biol Chem 274: 1533-1540.
    • (1999) J Biol Chem , vol.274 , pp. 1533-1540
    • Vito, P.1    Pellegrini, L.2    Guiet, C.3    D'Adamio, L.4
  • 32
    • 0037020677 scopus 로고    scopus 로고
    • The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner
    • Satoh H, Nakano Y, Shibata H, Maki M, (2002) The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner. Biochim Biophys Acta 1600: 61-67.
    • (2002) Biochim Biophys Acta , vol.1600 , pp. 61-67
    • Satoh, H.1    Nakano, Y.2    Shibata, H.3    Maki, M.4
  • 33
    • 27744432641 scopus 로고    scopus 로고
    • The penta-EF-hand protein ALG-2 interacts directly with the ESCRT-I component TSG101, and Ca2+-dependently co-localizes to aberrant endosomes with dominant-negative AAA ATPase SKD1/Vps4B
    • Katoh K, Suzuki H, Terasawa Y, Mizuno T, Yasuda J, et al. (2005) The penta-EF-hand protein ALG-2 interacts directly with the ESCRT-I component TSG101, and Ca2+-dependently co-localizes to aberrant endosomes with dominant-negative AAA ATPase SKD1/Vps4B. Biochem J 391: 677-685.
    • (2005) Biochem J , vol.391 , pp. 677-685
    • Katoh, K.1    Suzuki, H.2    Terasawa, Y.3    Mizuno, T.4    Yasuda, J.5
  • 34
    • 0032530396 scopus 로고    scopus 로고
    • The Golgi apparatus is an inositol 1,4,5-trisphosphate-sensitive Ca2+ store, with functional properties distinct from those of the endoplasmic reticulum
    • Pinton P, Pozzan T, Rizzuto R, (1998) The Golgi apparatus is an inositol 1,4,5-trisphosphate-sensitive Ca2+ store, with functional properties distinct from those of the endoplasmic reticulum. EMBO J 17: 5298-5308.
    • (1998) EMBO J , vol.17 , pp. 5298-5308
    • Pinton, P.1    Pozzan, T.2    Rizzuto, R.3
  • 35
    • 0035341345 scopus 로고    scopus 로고
    • The endoplasmic reticulum: one continuous or several separate Ca(2+) stores?
    • Petersen OH, Tepikin A, Park MK, (2001) The endoplasmic reticulum: one continuous or several separate Ca(2+) stores? Trends Neurosci 24: 271-276.
    • (2001) Trends Neurosci , vol.24 , pp. 271-276
    • Petersen, O.H.1    Tepikin, A.2    Park, M.K.3
  • 36
    • 0026527921 scopus 로고
    • Association of cytoplasmic free Ca2+ gradients with subcellular organelles
    • Wahl M, Sleight RG, Gruenstein E, (1992) Association of cytoplasmic free Ca2+ gradients with subcellular organelles. J Cell Physiol 150: 593-609.
    • (1992) J Cell Physiol , vol.150 , pp. 593-609
    • Wahl, M.1    Sleight, R.G.2    Gruenstein, E.3
  • 37
    • 0036878788 scopus 로고    scopus 로고
    • Calcium leak from intracellular stores-the enigma of calcium signalling
    • Camello C, Lomax R, Petersen OH, Tepikin AV, (2002) Calcium leak from intracellular stores-the enigma of calcium signalling. Cell Calcium 32: 355-361.
    • (2002) Cell Calcium , vol.32 , pp. 355-361
    • Camello, C.1    Lomax, R.2    Petersen, O.H.3    Tepikin, A.V.4
  • 38
    • 0030982434 scopus 로고    scopus 로고
    • High-resolution calcium mapping of the endoplasmic reticulum-Golgi-exocytic membrane system. Electron energy loss imaging analysis of quick frozen-freeze dried PC12 cells
    • Pezzati R, Bossi M, Podini P, Meldolesi J, Grohovaz F, (1997) High-resolution calcium mapping of the endoplasmic reticulum-Golgi-exocytic membrane system. Electron energy loss imaging analysis of quick frozen-freeze dried PC12 cells. Mol Biol Cell 8: 1501-1512.
    • (1997) Mol Biol Cell , vol.8 , pp. 1501-1512
    • Pezzati, R.1    Bossi, M.2    Podini, P.3    Meldolesi, J.4    Grohovaz, F.5
  • 39
    • 33847211759 scopus 로고    scopus 로고
    • TRAPPI tethers COPII vesicles by binding the coat subunit Sec23
    • Cai H, Yu S, Menon S, Cai Y, Lazarova D, et al. (2007) TRAPPI tethers COPII vesicles by binding the coat subunit Sec23. Nature 445: 941-944.
    • (2007) Nature , vol.445 , pp. 941-944
    • Cai, H.1    Yu, S.2    Menon, S.3    Cai, Y.4    Lazarova, D.5
  • 40
    • 18344405156 scopus 로고    scopus 로고
    • COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes
    • Matsuoka K, Orci L, Amherdt M, Bednarek SY, Hamamoto S, et al. (1998) COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell 93: 263-275.
    • (1998) Cell , vol.93 , pp. 263-275
    • Matsuoka, K.1    Orci, L.2    Amherdt, M.3    Bednarek, S.Y.4    Hamamoto, S.5
  • 41
    • 0347723909 scopus 로고    scopus 로고
    • Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting
    • Sato K, Nakano A, (2004) Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting. J Biol Chem 279: 1330-1335.
    • (2004) J Biol Chem , vol.279 , pp. 1330-1335
    • Sato, K.1    Nakano, A.2
  • 42
    • 79953754662 scopus 로고    scopus 로고
    • Sed4p stimulates Sar1p GTP hydrolysis and promotes limited coat disassembly
    • Kodera C, Yorimitsu T, Nakano A, Sato K, (2011) Sed4p stimulates Sar1p GTP hydrolysis and promotes limited coat disassembly. Traffic 12: 591-599.
    • (2011) Traffic , vol.12 , pp. 591-599
    • Kodera, C.1    Yorimitsu, T.2    Nakano, A.3    Sato, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.