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Volumn 207, Issue 6, 2014, Pages 695-703

Remodeling of secretory compartments creates CUPS during nutrient starvation

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEINS AND BINDING PROTEINS; COAT PROTEIN COMPLEX I; COAT PROTEIN COMPLEX II; GLUCOSE; GRH1 PROTEIN; MEMBRANE PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL KINASE; RAPAMYCIN; SED5 PROTEIN; UNCLASSIFIED DRUG; USO1 PROTEIN; CULTURE MEDIUM; GRH1 PROTEIN, S CEREVISIAE; GUANINE NUCLEOTIDE EXCHANGE FACTOR; PIK1 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; SEC7 GUANINE NUCLEOTIDE EXCHANGE FACTORS; SED5 PROTEIN, S CEREVISIAE; SYNTAXIN; USO1 PROTEIN, S CEREVISIAE; VESICULAR TRANSPORT PROTEIN;

EID: 84930445399     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201407119     Document Type: Article
Times cited : (46)

References (32)
  • 1
    • 0023746682 scopus 로고
    • SEC7 encodes an unusual, high molecular weight protein required for membrane traffic from the yeast Golgi apparatus
    • Achstetter, T., A. Franzusoff, C. Field, and R. Schekman. 1988. SEC7 encodes an unusual, high molecular weight protein required for membrane traffic from the yeast Golgi apparatus. J. Biol. Chem. 263:11711-11717.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11711-11717
    • Achstetter, T.1    Franzusoff, A.2    Field, C.3    Schekman, R.4
  • 2
    • 19644375795 scopus 로고    scopus 로고
    • Peptide signaling during terminal differentiation of Dictyostelium
    • Anjard, C., and W.F. Loomis. 2005. Peptide signaling during terminal differentiation of Dictyostelium. Proc. Natl. Acad. Sci. USA. 102:7607-7611. http://dx.doi.org/10.1073/pnas.0501820102
    • (2005) Proc. Natl. Acad. Sci. USA. , vol.102 , pp. 7607-7611
    • Anjard, C.1    Loomis, W.F.2
  • 3
    • 80053377675 scopus 로고    scopus 로고
    • Glucose regulates clathrin adaptors at the trans-Golgi network and endosomes
    • Aoh, Q.L., L.M. Graves, and M.C. Duncan. 2011. Glucose regulates clathrin adaptors at the trans-Golgi network and endosomes. Mol. Biol. Cell. 22:3671-3683. http://dx.doi.org/10.1091/mbc.E11-04-0309
    • (2011) Mol. Biol. Cell. , vol.22 , pp. 3671-3683
    • Aoh, Q.L.1    Graves, L.M.2    Duncan, M.C.3
  • 4
    • 0029024860 scopus 로고
    • A SNARE-like protein required for traffic through the Golgi complex
    • Banfield, D.K., M.J. Lewis, and H.R. Pelham. 1995. A SNARE-like protein required for traffic through the Golgi complex. Nature. 375:806-809. http://dx.doi.org/10.1038/375806a0
    • (1995) Nature. , vol.375 , pp. 806-809
    • Banfield, D.K.1    Lewis, M.J.2    Pelham, H.R.3
  • 5
    • 33846590554 scopus 로고    scopus 로고
    • The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi traffic
    • Behnia, R., F.A. Barr, J.J. Flanagan, C. Barlowe, and S. Munro. 2007. The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi traffic. J. Cell Biol. 176:255-261. http://dx .doi.org/10.1083/jcb.200607151
    • (2007) J. Cell Biol. , vol.176 , pp. 255-261
    • Behnia, R.1    Barr, F.A.2    Flanagan, J.J.3    Barlowe, C.4    Munro, S.5
  • 6
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • Bolte, S., and F.P. Cordelières. 2006. A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc. 224:213-232. http://dx.doi .org/10.1111/j.1365-2818.2006.01706.x
    • (2006) J. Microsc. , vol.224 , pp. 213-232
    • Bolte, S.1    Cordelières, F.P.2
  • 7
    • 84855490021 scopus 로고    scopus 로고
    • Biogenesis of a novel compartment for autophagosome-mediated unconventional protein secretion
    • Bruns, C., J.M. McCaffery, A.J. Curwin, J.M. Duran, and V. Malhotra. 2011. Biogenesis of a novel compartment for autophagosome-mediated unconventional protein secretion. J. Cell Biol. 195:979-992. http://dx.doi.org/ 10.1083/jcb.201106098
    • (2011) J. Cell Biol. , vol.195 , pp. 979-992
    • Bruns, C.1    McCaffery, J.M.2    Curwin, A.J.3    Duran, J.M.4    Malhotra, V.5
  • 8
    • 0032522377 scopus 로고    scopus 로고
    • Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins
    • Cao, X., N. Ballew, and C. Barlowe. 1998. Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO J. 17:2156-2165. http://dx.doi.org/10.1093/emboj/17.8.2156
    • (1998) EMBO J. , vol.17 , pp. 2156-2165
    • Cao, X.1    Ballew, N.2    Barlowe, C.3
  • 10
    • 77149155386 scopus 로고    scopus 로고
    • Unconventional secretion of Acb1 is mediated by autophagosomes
    • Duran, J.M., C. Anjard, C. Stefan, W.F. Loomis, and V. Malhotra. 2010. Unconventional secretion of Acb1 is mediated by autophagosomes. J. Cell Biol. 188:527-536. http://dx.doi.org/10.1083/jcb.200911154
    • (2010) J. Cell Biol. , vol.188 , pp. 527-536
    • Duran, J.M.1    Anjard, C.2    Stefan, C.3    Loomis, W.F.4    Malhotra, V.5
  • 11
    • 0026097957 scopus 로고
    • Localization of components involved in protein transport and processing through the yeast Golgi apparatus
    • Franzusoff, A., K. Redding, J. Crosby, R.S. Fuller, and R. Schekman. 1991. Localization of components involved in protein transport and processing through the yeast Golgi apparatus. J. Cell Biol. 112:27-37. http://dx.doi .org/10.1083/jcb.112.1.27
    • (1991) J. Cell Biol. , vol.112 , pp. 27-37
    • Franzusoff, A.1    Redding, K.2    Crosby, J.3    Fuller, R.S.4    Schekman, R.5
  • 12
    • 67349270900 scopus 로고    scopus 로고
    • Enzymatic assembly of DNA molecules up to several hundred kilobases
    • Gibson, D.G., L. Young, R.Y. Chuang, J.C. Venter, C.A. Hutchison III, and H.O. Smith. 2009. Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat. Methods. 6:343-345. http://dx.doi.org/10.1038/nmeth.1318
    • (2009) Nat. Methods. , vol.6 , pp. 343-345
    • Gibson, D.G.1    Young, L.2    Chuang, R.Y.3    Venter, J.C.4    Hutchison, C.A.5    Smith, H.O.6
  • 13
    • 84884487128 scopus 로고    scopus 로고
    • ER exit sites are physical and functional core autophagosome biogenesis components
    • Graef, M., J.R. Friedman, C. Graham, M. Babu, and J. Nunnari. 2013. ER exit sites are physical and functional core autophagosome biogenesis components. Mol. Biol. Cell. 24:2918-2931. http://dx.doi.org/10.1091/mbc.E13-07-0381
    • (2013) Mol. Biol. Cell. , vol.24 , pp. 2918-2931
    • Graef, M.1    Friedman, J.R.2    Graham, C.3    Babu, M.4    Nunnari, J.5
  • 14
    • 0026756118 scopus 로고
    • SED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex
    • Hardwick, K.G., and H.R. Pelham. 1992. SED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex. J. Cell Biol. 119:513-521. http://dx.doi.org/10.1083/ jcb.119.3.513
    • (1992) J. Cell Biol. , vol.119 , pp. 513-521
    • Hardwick, K.G.1    Pelham, H.R.2
  • 15
    • 0026620198 scopus 로고
    • SEC21 is a gene required for ER to Golgi protein transport that encodes a subunit of a yeast coatomer
    • Hosobuchi, M., T. Kreis, and R. Schekman. 1992. SEC21 is a gene required for ER to Golgi protein transport that encodes a subunit of a yeast coatomer. Nature. 360:603-605. http://dx.doi.org/10.1038/360603a0
    • (1992) Nature. , vol.360 , pp. 603-605
    • Hosobuchi, M.1    Kreis, T.2    Schekman, R.3
  • 17
    • 34547604776 scopus 로고    scopus 로고
    • The Golgi-associated protein GRASP is required for unconventional protein secretion during development
    • Kinseth, M.A., C. Anjard, D. Fuller, G. Guizzunti, W.F. Loomis, and V. Malhotra. 2007. The Golgi-associated protein GRASP is required for unconventional protein secretion during development. Cell. 130:524-534. http:// dx.doi.org/10.1016/j.cell.2007.06.029
    • (2007) Cell. , vol.130 , pp. 524-534
    • Kinseth, M.A.1    Anjard, C.2    Fuller, D.3    Guizzunti, G.4    Loomis, W.F.5    Malhotra, V.6
  • 18
    • 0028643562 scopus 로고
    • Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum
    • Letourneur, F., E.C. Gaynor, S. Hennecke, C. Démollière, R. Duden, S.D. Emr, H. Riezman, and P. Cosson. 1994. Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum. Cell. 79:1199- 1207. http://dx.doi.org/10.1016/0092-8674(94)90011-6
    • (1994) Cell. , vol.79 , pp. 1199-1207
    • Letourneur, F.1    Gaynor, E.C.2    Hennecke, S.3    Démollière, C.4    Duden, R.5    Emr, S.D.6    Riezman, H.7    Cosson, P.8
  • 19
    • 77955260357 scopus 로고    scopus 로고
    • The yeast GRASP Grh1 colocalizes with COPII and is dispensable for organizing the secretory pathway
    • Levi, S.K., D. Bhattacharyya, R.L. Strack, J.R. Austin II, and B.S. Glick. 2010. The yeast GRASP Grh1 colocalizes with COPII and is dispensable for organizing the secretory pathway. Traffic. 11:1168-1179. http://dx.doi .org/10.1111/j.1600-0854.2010.01089.x
    • (2010) Traffic. , vol.11 , pp. 1168-1179
    • Levi, S.K.1    Bhattacharyya, D.2    Strack, R.L.3    Austin, J.R.4    Glick, B.S.5
  • 20
    • 0030911653 scopus 로고    scopus 로고
    • A novel SNARE complex implicated in vesicle fusion with the endoplasmic reticulum
    • Lewis, M.J., J.C. Rayner, and H.R. Pelham. 1997. A novel SNARE complex implicated in vesicle fusion with the endoplasmic reticulum. EMBO J. 16:3017-3024. http://dx.doi.org/10.1093/emboj/16.11.3017
    • (1997) EMBO J. , vol.16 , pp. 3017-3024
    • Lewis, M.J.1    Rayner, J.C.2    Pelham, H.R.3
  • 21
    • 24344440195 scopus 로고    scopus 로고
    • Structure-based functional analysis reveals a role for the SM protein Sly1p in retrograde transport to the endoplasmic reticulum
    • Li, Y., D. Gallwitz, and R. Peng. 2005. Structure-based functional analysis reveals a role for the SM protein Sly1p in retrograde transport to the endoplasmic reticulum. Mol. Biol. Cell. 16:3951-3962. http://dx.doi.org/ 10.1091/mbc.E05-02-0114
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 3951-3962
    • Li, Y.1    Gallwitz, D.2    Peng, R.3
  • 23
    • 84879464160 scopus 로고    scopus 로고
    • Unconventional protein secretion: an evolving mechanism
    • Malhotra, V. 2013. Unconventional protein secretion: an evolving mechanism. EMBO J. 32:1660-1664. http://dx.doi.org/10.1038/emboj.2013.104
    • (2013) EMBO J. , vol.32 , pp. 1660-1664
    • Malhotra, V.1
  • 24
    • 77149152566 scopus 로고    scopus 로고
    • Unconventional secretion of Pichia pastoris Acb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation
    • Manjithaya, R., C. Anjard, W.F. Loomis, and S. Subramani. 2010. Unconventional secretion of Pichia pastoris Acb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation. J. Cell Biol. 188:537-546. http://dx.doi.org/10.1083/jcb.200911149
    • (2010) J. Cell Biol. , vol.188 , pp. 537-546
    • Manjithaya, R.1    Anjard, C.2    Loomis, W.F.3    Subramani, S.4
  • 25
    • 0025805962 scopus 로고
    • A cytoskeleton-related gene, uso1, is required for intracellular protein transport in Saccharomyces cerevisiae
    • Nakajima, H., A. Hirata, Y. Ogawa, T. Yonehara, K. Yoda, and M. Yamasaki. 1991. A cytoskeleton-related gene, uso1, is required for intracellular protein transport in Saccharomyces cerevisiae. J. Cell Biol. 113:245-260. http://dx.doi.org/10.1083/jcb.113.2.245
    • (1991) J. Cell Biol. , vol.113 , pp. 245-260
    • Nakajima, H.1    Hirata, A.2    Ogawa, Y.3    Yonehara, T.4    Yoda, K.5    Yamasaki, M.6
  • 26
    • 0032516856 scopus 로고    scopus 로고
    • SNAREs and membrane fusion in the Golgi apparatus
    • Nichols, B.J., and H.R. Pelham. 1998. SNAREs and membrane fusion in the Golgi apparatus. Biochim. Biophys. Acta. 1404:9-31. http://dx.doi.org/ 10.1016/S0167-4889(98)00044-5
    • (1998) Biochim. Biophys. Acta. , vol.1404 , pp. 9-31
    • Nichols, B.J.1    Pelham, H.R.2
  • 27
    • 84873531806 scopus 로고    scopus 로고
    • Diversity in unconventional protein secretion
    • Rabouille, C., V. Malhotra, and W. Nickel. 2012. Diversity in unconventional protein secretion. J. Cell Sci. 125:5251-5255. http://dx.doi.org/10.1242/ jcs.103630
    • (2012) J. Cell Sci. , vol.125 , pp. 5251-5255
    • Rabouille, C.1    Malhotra, V.2    Nickel, W.3
  • 28
    • 0031841313 scopus 로고    scopus 로고
    • Vam7p, a SNAP-25-like molecule, and Vam3p, a syntaxin homolog, function together in yeast vacuolar protein trafficking
    • Sato, T.K., T. Darsow, and S.D. Emr. 1998. Vam7p, a SNAP-25-like molecule, and Vam3p, a syntaxin homolog, function together in yeast vacuolar protein trafficking. Mol. Cell. Biol. 18:5308-5319.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5308-5319
    • Sato, T.K.1    Darsow, T.2    Emr, S.D.3
  • 29
    • 3042722112 scopus 로고    scopus 로고
    • Optimized cassettes for fluorescent protein tagging in Saccharomyces cerevisiae
    • Sheff, M.A., and K.S. Thorn. 2004. Optimized cassettes for fluorescent protein tagging in Saccharomyces cerevisiae. Yeast. 21:661-670. http://dx.doi .org/10.1002/yea.1130
    • (2004) Yeast. , vol.21 , pp. 661-670
    • Sheff, M.A.1    Thorn, K.S.2
  • 30
    • 47749141468 scopus 로고    scopus 로고
    • Signal-mediated dynamic retention of glycosyltransferases in the Golgi
    • Tu, L., W.C. Tai, L. Chen, and D.K. Banfield. 2008. Signal-mediated dynamic retention of glycosyltransferases in the Golgi. Science. 321:404-407. http://dx.doi.org/10.1126/science.1159411
    • (2008) Science. , vol.321 , pp. 404-407
    • Tu, L.1    Tai, W.C.2    Chen, L.3    Banfield, D.K.4
  • 31
    • 0033258472 scopus 로고    scopus 로고
    • The yeast phosphatidylinositol-4-OH kinase pik1 regulates secretion at the Golgi
    • Walch-Solimena, C., and P. Novick. 1999. The yeast phosphatidylinositol-4-OH kinase pik1 regulates secretion at the Golgi. Nat. Cell Biol. 1:523-525. http://dx.doi.org/10.1038/70319
    • (1999) Nat. Cell Biol. , vol.1 , pp. 523-525
    • Walch-Solimena, C.1    Novick, P.2
  • 32
    • 26244449794 scopus 로고    scopus 로고
    • Control of Golgi morphology and function by Sed5 t-SNARE phosphorylation
    • Weinberger, A., F. Kamena, R. Kama, A. Spang, and J.E. Gerst. 2005. Control of Golgi morphology and function by Sed5 t-SNARE phosphorylation. Mol. Biol. Cell. 16:4918-4930. http://dx.doi.org/10.1091/mbc.E05-02-0101
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 4918-4930
    • Weinberger, A.1    Kamena, F.2    Kama, R.3    Spang, A.4    Gerst, J.E.5


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