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Volumn 392, Issue 7, 2011, Pages 601-608

Cooperative and independent activities of Sgt2 and Get5 in the targeting of tail-anchored proteins

Author keywords

chaperone; GET pathway; Hsp70; protein quality control; protein targeting; TPR protein

Indexed keywords

CHAPERONE; GET5 PROTEIN; PROTEIN; SGT2 PROTEIN; UNCLASSIFIED DRUG;

EID: 79959440698     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2011.066     Document Type: Article
Times cited : (28)

References (19)
  • 1
    • 0034769599 scopus 로고    scopus 로고
    • Hsp104 interacts with Hsp90 cochaperones in respiring yeast
    • DOI 10.1128/MCB.21.22.7569-7575.2001
    • Abbas-Terki, T., Donze, O., Briand, P.A., and Picard, D. (2001).Hsp104 interacts with Hsp90 co-chaperones in respiring yeast. Mol. Cell Biol. 21, 7569-7575 (Pubitemid 32988768)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.22 , pp. 7569-7575
    • Abbas-Terki, T.1    Donze, O.2    Briand, P.-A.3    Picard, D.4
  • 3
    • 77953245945 scopus 로고    scopus 로고
    • Automated identification of pathways from quantitative genetic interaction data
    • Battle, A., Jonikas, M.C., Walter, P., Weissman, J.S., and Koller, D. (2010). Automated identification of pathways from quantitative genetic interaction data. Mol. Syst. Biol. 6, 379
    • (2010) Mol. Syst. Biol. , vol.6 , pp. 379
    • Battle, A.1    Jonikas, M.C.2    Walter, P.3    Weissman, J.S.4    Koller, D.5
  • 4
    • 60549104572 scopus 로고    scopus 로고
    • Remodelling of VipA VipB tubules by ClpVmediated threading is crucial for type VI protein secretion
    • Bonemann, G., Pietrosiuk, A., Diemand, A., Zentgraf, H., and Mogk, A. (2009). Remodelling of VipA/VipB tubules by ClpVmediated threading is crucial for type VI protein secretion. EMBO J. 28, 315-325
    • (2009) EMBO J. , vol.28 , pp. 315-325
    • Bonemann, G.1    Pietrosiuk, A.2    Diemand, A.3    Zentgraf, H.4    Mogk, A.5
  • 5
    • 77951209587 scopus 로고    scopus 로고
    • Crystal structure of Get4-Get5 complex and its interactions with Sgt2 Get3 and Ydj1
    • Chang, Y.W., Chuang, Y.C., Ho, Y.C., Cheng, M.Y., Sun, Y.J., Hsiao, C.D., and Wang, C. (2010). Crystal structure of Get4- Get5 complex and its interactions with Sgt2, Get3, and Ydj1 J. Biol. Chem. 285, 9962-9970
    • (2010) J. Biol. Chem. , vol.285 , pp. 9962-9970
    • Chang, Y.W.1    Chuang, Y.C.2    Ho, Y.C.3    Cheng, M.Y.4    Sun, Y.J.5    Hsiao, C.D.6    Wang, C.7
  • 7
    • 0344628648 scopus 로고    scopus 로고
    • TPR proteins: The versatile helix
    • DOI 10.1016/j.tibs.2003.10.007
    • D'Andrea, L.D. and Regan, L. (2003). TPR proteins: the versatile helix. Trends Biochem. Sci. 28, 655-662 (Pubitemid 37500900)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.12 , pp. 655-662
    • D'Andrea, L.D.1    Regan, L.2
  • 9
    • 4444271170 scopus 로고    scopus 로고
    • A versatile toolbox for PCR-based tagging of yeast genes: New fluorescent proteins, more markers and promoter substitution cassettes
    • DOI 10.1002/yea.1142
    • Janke, C., Magiera, M.M., Rathfelder, N., Taxis, C., Reber, S., Maekawa, H., Moreno-Borchart, A., Doenges, G., Schwob, E., Schiebel, E., et al. (2004). A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes. Yeast 21, 947-962 (Pubitemid 39206863)
    • (2004) Yeast , vol.21 , Issue.11 , pp. 947-962
    • Janke, C.1    Magiera, M.M.2    Rathfelder, N.3    Taxis, C.4    Reber, S.5    Maekawa, H.6    Moreno-Borchart, A.7    Doenges, G.8    Schwob, E.9    Schiebel, E.10    Knop, M.11
  • 11
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • Kampinga, H.H. and Craig, E.A. (2010). The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat. Rev. Mol. Cell Biol. 11, 579-592
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 12
    • 34250862251 scopus 로고    scopus 로고
    • SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae
    • DOI 10.1379/CSC-220R.1
    • Liou, S.T., Cheng, M.Y., and Wang, C. (2007). SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae. Cell Stress Chaperones 12, 59-70 (Pubitemid 47403329)
    • (2007) Cell Stress and Chaperones , vol.12 , Issue.1 , pp. 59-70
    • Liou, S.-T.1    Cheng, M.-Y.2    Wang, C.3
  • 13
    • 33745749328 scopus 로고    scopus 로고
    • Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor
    • DOI 10.1038/sj.emboj.7601139, PII 7601139
    • Raviol, H., Sadlish, H., Rodriguez, F., Mayer, M.P., and Bukau, B. (2006). Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J. 25, 2510-2518 (Pubitemid 44012233)
    • (2006) EMBO Journal , vol.25 , Issue.11 , pp. 2510-2518
    • Raviol, H.1    Sadlish, H.2    Rodriguez, F.3    Mayer, M.P.4    Bukau, B.5
  • 15
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • DOI 10.1016/S0092-8674(00)80830-2
    • Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F.U., and Moarefi, I. (2000). Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101, 199-210 (Pubitemid 32004747)
    • (2000) Cell , vol.101 , Issue.2 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl F.Ulrich7    Moarefi, I.8
  • 17
    • 19544363062 scopus 로고    scopus 로고
    • Prions as adaptive conduits of memory and inheritance
    • DOI 10.1038/nrg1616
    • Shorter, J. and Lindquist, S. (2005). Prions as adaptive conduits of memory and inheritance. Nat. Rev. Genet. 6, 435-450 (Pubitemid 40733889)
    • (2005) Nature Reviews Genetics , vol.6 , Issue.6 , pp. 435-450
    • Shorter, J.1    Lindquist, S.2
  • 18
    • 55949109442 scopus 로고    scopus 로고
    • In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104
    • Tipton, K.A., Verges, K.J., and Weissman, J.S. (2008). In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104 Mol. Cell 32, 584-591
    • (2008) Mol. Cell , vol.32 , pp. 584-591
    • Tipton, K.A.1    Verges, K.J.2    Weissman, J.S.3
  • 19
    • 77957376226 scopus 로고    scopus 로고
    • A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum
    • Wang, F., Brown, E.C., Mak, G., Zhuang, J., and Denic, V. (2010). A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol. Cell 40, 159-171
    • (2010) Mol. Cell , vol.40 , pp. 159-171
    • Wang, F.1    Brown, E.C.2    Mak, G.3    Zhuang, J.4    Denic, V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.