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Volumn 174, Issue 1, 2006, Pages 19-25

Palmitoylation by the DHHC protein Pfa4 regulates the ER exit of Chs3

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; ASPARTYLHISTIDYLHISTIDYLCYSTEINE; CHAPERONE; CHITIN SYNTHASE; MEMBRANE PROTEIN; PROTEIN ACYLTRANSFERASES; PROTEIN CHS3; PROTEIN CHS7; PROTEIN PFA4; UNCLASSIFIED DRUG;

EID: 33745623380     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200602049     Document Type: Article
Times cited : (95)

References (31)
  • 1
    • 0037213362 scopus 로고    scopus 로고
    • The on-off story of protein palmitoylation
    • Bijlmakers, M.J., and M. Marsh. 2003. The on-off story of protein palmitoylation. Trends Cell Biol. 13:32-42.
    • (2003) Trends Cell Biol. , vol.13 , pp. 32-42
    • Bijlmakers, M.J.1    Marsh, M.2
  • 2
    • 0033972955 scopus 로고    scopus 로고
    • Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late Golgi
    • Conibear, E., and T.H. Stevens. 2000. Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late Golgi. Mol. Biol. Cell. 11:305-323.
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 305-323
    • Conibear, E.1    Stevens, T.H.2
  • 4
    • 0031714661 scopus 로고    scopus 로고
    • Molecular analysis of Chs3p participation in chitin synthase III activity
    • Cos, T., R.A. Ford, J.A. Trilla, A. Duran, E. Cabib, and C. Roncero. 1998. Molecular analysis of Chs3p participation in chitin synthase III activity. Eur. J. Biochem. 256:419-426.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 419-426
    • Cos, T.1    Ford, R.A.2    Trilla, J.A.3    Duran, A.4    Cabib, E.5    Roncero, C.6
  • 5
    • 0842266659 scopus 로고    scopus 로고
    • Labeling and quantifying sites of protein palmitoylation
    • Drisdel, R.C., and W.N. Green. 2004. Labeling and quantifying sites of protein palmitoylation. Biotechniques. 36:276-285.
    • (2004) Biotechniques , vol.36 , pp. 276-285
    • Drisdel, R.C.1    Green, W.N.2
  • 6
    • 9244247297 scopus 로고    scopus 로고
    • The role of palmitoylation in functional expression of nicotinic alpha7 receptors
    • Drisdel, R.C., E. Manzana, and W.N. Green. 2004. The role of palmitoylation in functional expression of nicotinic alpha7 receptors. J. Neurosci. 24:10502-10510.
    • (2004) J. Neurosci. , vol.24 , pp. 10502-10510
    • Drisdel, R.C.1    Manzana, E.2    Green, W.N.3
  • 7
    • 0032743154 scopus 로고    scopus 로고
    • Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesicles
    • Gilstring, C.F., M. Melin-Larsson, and P.O. Ljungdahl. 1999. Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesicles. Mol. Biol. Cell. 10:3549-3565.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 3549-3565
    • Gilstring, C.F.1    Melin-Larsson, M.2    Ljungdahl, P.O.3
  • 10
    • 12144251018 scopus 로고    scopus 로고
    • Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the ER
    • Kota, J., and P.O. Ljungdahl. 2005. Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the ER. J. Cell Biol. 168:79-88.
    • (2005) J. Cell Biol. , vol.168 , pp. 79-88
    • Kota, J.1    Ljungdahl, P.O.2
  • 11
    • 2942620604 scopus 로고    scopus 로고
    • Analysis of beta-1,3-glucan assembly in Saccharomyces cerevisiae using a synthetic interaction network and altered sensitivity to caspofungin
    • Lesage, G., A.M. Sdicu, P. Menard, J. Shapiro, S. Hussein, and H. Bussey. 2004. Analysis of beta-1,3-glucan assembly in Saccharomyces cerevisiae using a synthetic interaction network and altered sensitivity to caspofungin. Genetics. 167:35-49.
    • (2004) Genetics , vol.167 , pp. 35-49
    • Lesage, G.1    Sdicu, A.M.2    Menard, P.3    Shapiro, J.4    Hussein, S.5    Bussey, H.6
  • 12
    • 0033944545 scopus 로고    scopus 로고
    • Inositol phosphorylceramide synthase is located in the Golgi apparatus of Saccharomyces cerevisiae
    • Levine, T.P., C.A. Wiggins, and S. Munro. 2000. Inositol phosphorylceramide synthase is located in the Golgi apparatus of Saccharomyces cerevisiae. Mol. Biol. Cell. 11:2267-2281.
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 2267-2281
    • Levine, T.P.1    Wiggins, C.A.2    Munro, S.3
  • 13
    • 0037174987 scopus 로고    scopus 로고
    • Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae
    • Lobo, S., W.K. Greentree, M.E. Linder, and R.J. Deschenes. 2002. Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae. J. Biol. Chem. 277:41268-41273.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41268-41273
    • Lobo, S.1    Greentree, W.K.2    Linder, M.E.3    Deschenes, R.J.4
  • 14
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M.S., A. McKenzie III, D.J. Demarini, N.G. Shah, A. Wach, A. Brachat, P. Philippsen, and J.R. Pringle. 1998. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast. 14:953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 15
    • 6344272891 scopus 로고    scopus 로고
    • Role of Vma21p in assembly and transport of the yeast vacuolar ATPase
    • Malkus, P., L.A. Graham, T.H. Stevens, and R. Schekman. 2004. Role of Vma21p in assembly and transport of the yeast vacuolar ATPase. Mol. Biol. Cell. 15:5075-5091.
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 5075-5091
    • Malkus, P.1    Graham, L.A.2    Stevens, T.H.3    Schekman, R.4
  • 17
    • 33744826797 scopus 로고    scopus 로고
    • Protein palmitoylation by a family of DHHC protein S-acyltransferases
    • Mitchell, D.A., A. Vasudevan, M.E. Linder, and R.J. Deschenes. 2006. Protein palmitoylation by a family of DHHC protein S-acyltransferases. J. Lipid Res. 47:1118-1127.
    • (2006) J. Lipid Res. , vol.47 , pp. 1118-1127
    • Mitchell, D.A.1    Vasudevan, A.2    Linder, M.E.3    Deschenes, R.J.4
  • 18
    • 15044343147 scopus 로고    scopus 로고
    • Transmembrane topology of the protein palmitoyl transferase Akr1
    • Politis, E.G., A.F. Roth, and N.G. Davis. 2005. Transmembrane topology of the protein palmitoyl transferase Akr1. J. Biol. Chem. 280:10156-10163.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10156-10163
    • Politis, E.G.1    Roth, A.F.2    Davis, N.G.3
  • 19
    • 0036935611 scopus 로고    scopus 로고
    • The genetic complexity of chitin synthesis in fungi
    • Roncero, C. 2002. The genetic complexity of chitin synthesis in fungi. Curr. Genet. 41:367-378.
    • (2002) Curr. Genet. , vol.41 , pp. 367-378
    • Roncero, C.1
  • 20
    • 0021965293 scopus 로고
    • Effect of Calcofluor white and Congo red on fungal cell wall morphogenesis: In vivo activation of chitin polymerization
    • Roncero, C., and A. Duran. 1985. Effect of Calcofluor white and Congo red on fungal cell wall morphogenesis: in vivo activation of chitin polymerization. J. Bacteriol. 163:1180-1185.
    • (1985) J. Bacteriol. , vol.163 , pp. 1180-1185
    • Roncero, C.1    Duran, A.2
  • 21
    • 0037078323 scopus 로고    scopus 로고
    • The yeast DHHC cysteinerich domain protein Akr1p is a palmitoyl transferase
    • Roth, A.F., Y. Feng, L. Chen, and N.G. Davis. 2002. The yeast DHHC cysteinerich domain protein Akr1p is a palmitoyl transferase. J. Cell Biol. 159:23-28.
    • (2002) J. Cell Biol. , vol.159 , pp. 23-28
    • Roth, A.F.1    Feng, Y.2    Chen, L.3    Davis, N.G.4
  • 23
    • 4544328860 scopus 로고    scopus 로고
    • The early stages of the intracellular transport of membrane proteins: Clinical and pharmacological implications
    • Schulein, R. 2004. The early stages of the intracellular transport of membrane proteins: clinical and pharmacological implications. Rev. Physiol. Biochem. Pharmacol. 151:45-91.
    • (2004) Rev. Physiol. Biochem. Pharmacol. , vol.151 , pp. 45-91
    • Schulein, R.1
  • 24
    • 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.
    • (2004) Yeast , vol.21 , pp. 661-670
    • Sheff, M.A.1    Thorn, K.S.2
  • 25
    • 25444491476 scopus 로고    scopus 로고
    • The vacuolar DHHC-CRD protein Pfa3p is a protein acyltransferase for Vac8p
    • Smotrys, J.E., M.J. Schoenfish, M.A. Stutz, and M.E. Linder. 2005. The vacuolar DHHC-CRD protein Pfa3p is a protein acyltransferase for Vac8p. J. Cell Biol. 170:1091-1099.
    • (2005) J. Cell Biol. , vol.170 , pp. 1091-1099
    • Smotrys, J.E.1    Schoenfish, M.J.2    Stutz, M.A.3    Linder, M.E.4
  • 27
    • 0033553884 scopus 로고    scopus 로고
    • Chs7p, a new protein involved in the control of protein export from the endoplasmic reticulum that is specifically engaged in the regulation of chitin synthesis in Saccharomyces cerevisiae
    • Trilla, J.A., A. Duran, and C. Roncero. 1999. Chs7p, a new protein involved in the control of protein export from the endoplasmic reticulum that is specifically engaged in the regulation of chitin synthesis in Saccharomyces cerevisiae. J. Cell Biol. 145:1153-1163.
    • (1999) J. Cell Biol. , vol.145 , pp. 1153-1163
    • Trilla, J.A.1    Duran, A.2    Roncero, C.3
  • 28
    • 23044444831 scopus 로고    scopus 로고
    • Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation
    • Valdez-Taubas, J., and H. Pelham. 2005. Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation. EMBO J. 24:2524-2532.
    • (2005) EMBO J. , vol.24 , pp. 2524-2532
    • Valdez-Taubas, J.1    Pelham, H.2
  • 29
    • 0042838332 scopus 로고    scopus 로고
    • The yeasts Rho1p and Pkc1p regulate the transport of chitin synthase III (Chs3p) from internal stores to the plasma membrane
    • Valdivia, R.H., and R. Schekman. 2003. The yeasts Rho1p and Pkc1p regulate the transport of chitin synthase III (Chs3p) from internal stores to the plasma membrane. Proc. Natl. Acad. Sci. USA. 100:10287-10292.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10287-10292
    • Valdivia, R.H.1    Schekman, R.2
  • 30
    • 0029808478 scopus 로고    scopus 로고
    • Chs1p and Chs3p, two proteins involved in chitin synthesis, populate a compartment of the Saccharomyces cerevisiae endocytic pathway
    • Ziman, M., J.S. Chuang, and R.W. Schekman. 1996. Chs1p and Chs3p, two proteins involved in chitin synthesis, populate a compartment of the Saccharomyces cerevisiae endocytic pathway. Mol. Biol. Cell. 7:1909-1919.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 1909-1919
    • Ziman, M.1    Chuang, J.S.2    Schekman, R.W.3
  • 31
    • 0031866442 scopus 로고    scopus 로고
    • Chs6p-dependent anterograde transport of Chs3p from the chitosome to the plasma membrane in Saccharomyces cerevisiae
    • Ziman, M., J.S. Chuang, M. Tsung, S. Hamamoto, and R. Schekman. 1998. Chs6p-dependent anterograde transport of Chs3p from the chitosome to the plasma membrane in Saccharomyces cerevisiae. Mol. Biol. Cell. 9:1565-1576.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 1565-1576
    • Ziman, M.1    Chuang, J.S.2    Tsung, M.3    Hamamoto, S.4    Schekman, R.5


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