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Volumn 587, Issue 19, 2013, Pages 3261-3266

Endoplasmic Reticulum stress reduces COPII vesicle formation and modifies Sec23a cycling at ERESs

Author keywords

COPII; ER stress; ERES; Sec23

Indexed keywords

COAT PROTEIN COMPLEX II; GUANINE NUCLEOTIDE EXCHANGE FACTOR; SEC23A PROTEIN; UNCLASSIFIED DRUG;

EID: 84884280837     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.08.021     Document Type: Article
Times cited : (27)

References (41)
  • 1
    • 33750969692 scopus 로고    scopus 로고
    • Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells
    • P. Watson, A.K. Townley, P. Koka, K.J. Palmer, and D.J. Stephens Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells Traffic 7 2006 1678 1687
    • (2006) Traffic , vol.7 , pp. 1678-1687
    • Watson, P.1    Townley, A.K.2    Koka, P.3    Palmer, K.J.4    Stephens, D.J.5
  • 2
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • G. Palade Intracellular aspects of the process of protein synthesis Science 189 1975 347 358
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.1
  • 4
    • 10144220633 scopus 로고    scopus 로고
    • The organization of endoplasmic reticulum export complexes
    • S.I. Bannykh, T. Rowe, and W.E. Balch The organization of endoplasmic reticulum export complexes J. Cell Biol. 135 1996 19 35
    • (1996) J. Cell Biol. , vol.135 , pp. 19-35
    • Bannykh, S.I.1    Rowe, T.2    Balch, W.E.3
  • 5
    • 0030222342 scopus 로고    scopus 로고
    • Principles of selective transport: Coat complexes hold the key
    • M. Aridor, and W.E. Balch Principles of selective transport: coat complexes hold the key Trends Cell Biol. 6 1996 315 320
    • (1996) Trends Cell Biol. , vol.6 , pp. 315-320
    • Aridor, M.1    Balch, W.E.2
  • 6
    • 0027500969 scopus 로고
    • SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER
    • C. Barlowe, and R. Schekman SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER Nature 365 1993 347 349
    • (1993) Nature , vol.365 , pp. 347-349
    • Barlowe, C.1    Schekman, R.2
  • 7
    • 0035141907 scopus 로고    scopus 로고
    • Purification and properties of rat liver Sec23-Sec24 complex
    • J.T. Weissman, M. Aridor, and W.E. Balch Purification and properties of rat liver Sec23-Sec24 complex Methods Enzymol. 329 2001 431 438
    • (2001) Methods Enzymol. , vol.329 , pp. 431-438
    • Weissman, J.T.1    Aridor, M.2    Balch, W.E.3
  • 8
    • 0037112755 scopus 로고    scopus 로고
    • Cargo selection into COPII vesicles is driven by the Sec24p subunit
    • E. Miller, B. Antonny, S. Hamamoto, and R. Schekman Cargo selection into COPII vesicles is driven by the Sec24p subunit EMBO J. 21 2002 6105 6113
    • (2002) EMBO J. , vol.21 , pp. 6105-6113
    • Miller, E.1    Antonny, B.2    Hamamoto, S.3    Schekman, R.4
  • 9
    • 23944488301 scopus 로고    scopus 로고
    • Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle
    • M.C. Lee, L. Orci, S. Hamamoto, E. Futai, M. Ravazzola, and R. Schekman Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle Cell 122 2005 605 617
    • (2005) Cell , vol.122 , pp. 605-617
    • Lee, M.C.1    Orci, L.2    Hamamoto, S.3    Futai, E.4    Ravazzola, M.5    Schekman, R.6
  • 10
    • 0027082971 scopus 로고
    • Sec23p and a novel 105-kDa protein function as a multimeric complex to promote vesicle budding and protein transport from the endoplasmic reticulum
    • L. Hicke, T. Yoshihisa, and R. Schekman Sec23p and a novel 105-kDa protein function as a multimeric complex to promote vesicle budding and protein transport from the endoplasmic reticulum Mol. Biol. Cell 3 1992 667 676
    • (1992) Mol. Biol. Cell , vol.3 , pp. 667-676
    • Hicke, L.1    Yoshihisa, T.2    Schekman, R.3
  • 11
    • 0028233498 scopus 로고
    • COPII: A membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum
    • C. Barlowe COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum Cell 77 1994 895 907
    • (1994) Cell , vol.77 , pp. 895-907
    • Barlowe, C.1
  • 12
    • 34250745253 scopus 로고    scopus 로고
    • Structure and organization of coat proteins in the COPII cage
    • S. Fath, J.D. Mancias, X. Bi, and J. Goldberg Structure and organization of coat proteins in the COPII cage Cell 129 2007 1325 1336
    • (2007) Cell , vol.129 , pp. 1325-1336
    • Fath, S.1    Mancias, J.D.2    Bi, X.3    Goldberg, J.4
  • 14
    • 0028803617 scopus 로고
    • Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p
    • P. Espenshade, R.E. Gimeno, E. Holzmacher, P. Teung, and C.A. Kaiser Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p J. Cell Biol. 131 1995 311 324
    • (1995) J. Cell Biol. , vol.131 , pp. 311-324
    • Espenshade, P.1    Gimeno, R.E.2    Holzmacher, E.3    Teung, P.4    Kaiser, C.A.5
  • 15
    • 0037119988 scopus 로고    scopus 로고
    • Sec16p potentiates the action of COPII proteins to bud transport vesicles
    • F. Supek, D.T. Madden, S. Hamamoto, L. Orci, and R. Schekman Sec16p potentiates the action of COPII proteins to bud transport vesicles J. Cell Biol. 158 2002 1029 1038
    • (2002) J. Cell Biol. , vol.158 , pp. 1029-1038
    • Supek, F.1    Madden, D.T.2    Hamamoto, S.3    Orci, L.4    Schekman, R.5
  • 16
    • 84856884587 scopus 로고    scopus 로고
    • Sec24p and Sec16p cooperate to regulate the GTP cycle of the COPII coat
    • L.F. Kung Sec24p and Sec16p cooperate to regulate the GTP cycle of the COPII coat EMBO J. 31 2012 1014 1027
    • (2012) EMBO J. , vol.31 , pp. 1014-1027
    • Kung, L.F.1
  • 17
    • 84863830464 scopus 로고    scopus 로고
    • Insights into structural and regulatory roles of Sec16 in COPII vesicle formation at ER exit sites
    • T. Yorimitsu, and K. Sato Insights into structural and regulatory roles of Sec16 in COPII vesicle formation at ER exit sites Mol. Biol. Cell 23 2012 2930 2942
    • (2012) Mol. Biol. Cell , vol.23 , pp. 2930-2942
    • Yorimitsu, T.1    Sato, K.2
  • 18
    • 29144454715 scopus 로고    scopus 로고
    • Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission
    • A. Bielli, C.J. Haney, G. Gabreski, S.C. Watkins, S.I. Bannykh, and M. Aridor Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission J. Cell Biol. 171 2005 919 924
    • (2005) J. Cell Biol. , vol.171 , pp. 919-924
    • Bielli, A.1    Haney, C.J.2    Gabreski, G.3    Watkins, S.C.4    Bannykh, S.I.5    Aridor, M.6
  • 19
    • 0027467609 scopus 로고
    • Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum
    • T. Yoshihisa, C. Barlowe, and R. Schekman Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum Science 259 1993 1466 1468
    • (1993) Science , vol.259 , pp. 1466-1468
    • Yoshihisa, T.1    Barlowe, C.2    Schekman, R.3
  • 20
    • 18344405156 scopus 로고    scopus 로고
    • COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes
    • K. Matsuoka, L. Orci, M. Amherdt, S.Y. Bednarek, S. Hamamoto, R. Schekman, and T. Yeung COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes Cell 93 1998 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    Schekman, R.6    Yeung, T.7
  • 22
    • 49149100705 scopus 로고    scopus 로고
    • Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load
    • H. Farhan, M. Weiss, K. Tani, R.J. Kaufman, and H.P. Hauri Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load EMBO J. 27 2008 2043 2054
    • (2008) EMBO J. , vol.27 , pp. 2043-2054
    • Farhan, H.1    Weiss, M.2    Tani, K.3    Kaufman, R.J.4    Hauri, H.P.5
  • 23
    • 70350763840 scopus 로고    scopus 로고
    • Visualization of cargo concentration by COPII minimal machinery in a planar lipid membrane
    • K.V. Tabata, K. Sato, T. Ide, T. Nishizaka, A. Nakano, and H. Noji Visualization of cargo concentration by COPII minimal machinery in a planar lipid membrane EMBO J. 28 2009 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    Noji, H.6
  • 24
    • 20144377947 scopus 로고    scopus 로고
    • P125 is localized in endoplasmic reticulum exit sites and involved in their organization
    • W. Shimoi P125 is localized in endoplasmic reticulum exit sites and involved in their organization J. Biol. Chem. 280 2005 10141 10148
    • (2005) J. Biol. Chem. , vol.280 , pp. 10141-10148
    • Shimoi, W.1
  • 25
    • 33846025382 scopus 로고    scopus 로고
    • ALG-2 directly binds Sec31A and localizes at endoplasmic reticulum exit sites in a Ca2+-dependent manner
    • H. Shibata, H. Suzuki, H. Yoshida, and M. Maki ALG-2 directly binds Sec31A and localizes at endoplasmic reticulum exit sites in a Ca2+-dependent manner Biochem. Biophys. Res. Commun. 353 2007 756 763
    • (2007) Biochem. Biophys. Res. Commun. , vol.353 , pp. 756-763
    • Shibata, H.1    Suzuki, H.2    Yoshida, H.3    Maki, M.4
  • 26
    • 79955642453 scopus 로고    scopus 로고
    • TFG-1 function in protein secretion and oncogenesis
    • K. Witte TFG-1 function in protein secretion and oncogenesis Nat. Cell Biol. 13 2011 550 558
    • (2011) Nat. Cell Biol. , vol.13 , pp. 550-558
    • Witte, K.1
  • 27
    • 84876387069 scopus 로고    scopus 로고
    • Secretory protein biogenesis and traffic in the early secretory pathway
    • C.K. Barlowe, and E.A. Miller Secretory protein biogenesis and traffic in the early secretory pathway Genetics 193 2013 383 410
    • (2013) Genetics , vol.193 , pp. 383-410
    • Barlowe, C.K.1    Miller, E.A.2
  • 28
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • D. Ron, and P. Walter Signal integration in the endoplasmic reticulum unfolded protein response Nat. Rev. Mol. Cell Biol. 8 2007 519 529
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 29
    • 10444226462 scopus 로고    scopus 로고
    • ER stress and the unfolded protein response
    • M. Schroder, and R.J. Kaufman ER stress and the unfolded protein response Mutat. Res. 569 2005 29 63
    • (2005) Mutat. Res. , vol.569 , pp. 29-63
    • Schroder, M.1    Kaufman, R.J.2
  • 30
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • I. Tabas, and D. Ron Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress Nat. Cell Biol. 13 2011 184 190
    • (2011) Nat. Cell Biol. , vol.13 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 32
    • 33748690946 scopus 로고    scopus 로고
    • Nitric oxide-induced endoplasmic reticulum stress activates the expression of cargo receptor proteins and alters the glycoprotein transport to the Golgi complex
    • M. Renna, R. Faraonio, S. Bonatti, D. De Stefano, R. Carnuccio, G. Tajana, and P. Remondelli Nitric oxide-induced endoplasmic reticulum stress activates the expression of cargo receptor proteins and alters the glycoprotein transport to the Golgi complex Int. J. Biochem. Cell Biol. 38 2006 2040 2048
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 2040-2048
    • Renna, M.1    Faraonio, R.2    Bonatti, S.3    De Stefano, D.4    Carnuccio, R.5    Tajana, G.6    Remondelli, P.7
  • 33
    • 34547961744 scopus 로고    scopus 로고
    • Regulation of ERGIC-53 gene transcription in response to endoplasmic reticulum stress
    • M. Renna, M.G. Caporaso, S. Bonatti, R.J. Kaufman, and P. Remondelli Regulation of ERGIC-53 gene transcription in response to endoplasmic reticulum stress J. Biol. Chem. 282 2007 22499 22512
    • (2007) J. Biol. Chem. , vol.282 , pp. 22499-22512
    • Renna, M.1    Caporaso, M.G.2    Bonatti, S.3    Kaufman, R.J.4    Remondelli, P.5
  • 34
    • 70350323730 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress reduces the export from the ER and alters the architecture of post-ER compartments
    • G. Amodio Endoplasmic reticulum stress reduces the export from the ER and alters the architecture of post-ER compartments Int. J. Biochem. Cell Biol. 41 2009 2511 2521
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 2511-2521
    • Amodio, G.1
  • 35
    • 0035203528 scopus 로고    scopus 로고
    • The GM130 and GRASP65 Golgi proteins cycle through and define a subdomain of the intermediate compartment
    • P. Marra The GM130 and GRASP65 Golgi proteins cycle through and define a subdomain of the intermediate compartment Nat. Cell Biol. 3 2001 1101 1113
    • (2001) Nat. Cell Biol. , vol.3 , pp. 1101-1113
    • Marra, P.1
  • 36
    • 0027179841 scopus 로고
    • Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex
    • M.A. De Matteis, G. Santini, R.A. Kahn, G. Di Tullio, and A. Luini Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex Nature 364 1993 818 821
    • (1993) Nature , vol.364 , pp. 818-821
    • De Matteis, M.A.1    Santini, G.2    Kahn, R.A.3    Di Tullio, G.4    Luini, A.5
  • 38
    • 70350031753 scopus 로고    scopus 로고
    • Organisation of human ER-exit sites: Requirements for the localisation of Sec16 to transitional ER
    • H. Hughes Organisation of human ER-exit sites: requirements for the localisation of Sec16 to transitional ER J. Cell Sci. 122 2009 2924 2934
    • (2009) J. Cell Sci. , vol.122 , pp. 2924-2934
    • Hughes, H.1
  • 39
    • 33847211759 scopus 로고    scopus 로고
    • TRAPPI tethers COPII vesicles by binding the coat subunit Sec23
    • H. Cai TRAPPI tethers COPII vesicles by binding the coat subunit Sec23 Nature 445 2007 941 944
    • (2007) Nature , vol.445 , pp. 941-944
    • Cai, H.1
  • 41
    • 0038387865 scopus 로고    scopus 로고
    • Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23
    • M. Cohen, F. Stutz, N. Belgareh, R. Haguenauer-Tsapis, and C. Dargemont Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23 Nat. Cell Biol. 5 2003 661 667
    • (2003) Nat. Cell Biol. , vol.5 , pp. 661-667
    • Cohen, M.1    Stutz, F.2    Belgareh, N.3    Haguenauer-Tsapis, R.4    Dargemont, C.5


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