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Volumn 5, Issue 7, 2004, Pages 692-697

A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation

Author keywords

Dsk2p; ER associated degradation; Proteasome; Rad23p; Ubiquitin

Indexed keywords

BINDING PROTEIN; CARRIER PROTEIN; DSK2 PROTEIN; GENE PRODUCT; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; MEMBRANE PROTEIN; PROTEASOME; RAD23 PROTEIN; UNCLASSIFIED DRUG;

EID: 4444320698     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.embor.7400164     Document Type: Article
Times cited : (182)

References (28)
  • 1
    • 0029985369 scopus 로고    scopus 로고
    • Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway
    • Biederer T, Volkwein C, Sommer T (1996) Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway. EMBO J 15: 2069-2076
    • (1996) EMBO J. , vol.15 , pp. 2069-2076
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3
  • 2
    • 0030015075 scopus 로고    scopus 로고
    • Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center
    • Biggins S, Ivanovska I, Rose MD (1996) Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center. J Cell Biol 133: 1331-1346
    • (1996) J. Cell Biol. , vol.133 , pp. 1331-1346
    • Biggins, S.1    Ivanovska, I.2    Rose, M.D.3
  • 3
    • 0031885043 scopus 로고    scopus 로고
    • Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins
    • Bordallo J, Plemper RK, Finger A, Wolf DH (1998) Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins. Mol Biol Cell 9: 209-222
    • (1998) Mol. Biol. Cell , vol.9 , pp. 209-222
    • Bordallo, J.1    Plemper, R.K.2    Finger, A.3    Wolf, D.H.4
  • 4
    • 0036277299 scopus 로고    scopus 로고
    • Rad23 promotes the targeting of proteolytic substrates to the proteasome
    • Chen L, Madura K (2002) Rad23 promotes the targeting of proteolytic substrates to the proteasome. Mol Cell Biol 22: 4902-4913
    • (2002) Mol. Cell Biol. , vol.22 , pp. 4902-4913
    • Chen, L.1    Madura, K.2
  • 5
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard L, Molinari M, Helenius A (1999) Setting the standards: quality control in the secretory pathway. Science 286: 1882-1888
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 6
    • 0033780610 scopus 로고    scopus 로고
    • A regulatory link between ER-associated protein degradation and the unfolded-protein response
    • Friedländer R, Jarosch E, Urban J, Volkwein C, Sommer T (2000) A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat Cell Biol 2: 379-384
    • (2000) Nat. Cell Biol. , vol.2 , pp. 379-384
    • Friedländer, R.1    Jarosch, E.2    Urban, J.3    Volkwein, C.4    Sommer, T.5
  • 7
    • 0031890210 scopus 로고    scopus 로고
    • Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26S proteasome subunit Mcb1
    • Fu H et al (1998) Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26S proteasome subunit Mcb1. J Biol Chem 273: 1970-1981
    • (1998) J. Biol. Chem. , vol.273 , pp. 1970-1981
    • Fu, H.1
  • 8
    • 0037154160 scopus 로고    scopus 로고
    • Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
    • Funakoshi M, Sasaki T, Nishimoto T, Kobayashi H (2002) Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc Natl Acad Sci USA 99: 745-750
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 745-750
    • Funakoshi, M.1    Sasaki, T.2    Nishimoto, T.3    Kobayashi, H.4
  • 9
    • 0027220740 scopus 로고
    • Promoter elements determining weak expression of the GAL4 regulatory gene of Saccharomyces cerevisiae
    • Griggs DW, Johnston M (1993) Promoter elements determining weak expression of the GAL4 regulatory gene of Saccharomyces cerevisiae. Mol Cell Biol 13: 4999-5009
    • (1993) Mol. Cell Biol. , vol.13 , pp. 4999-5009
    • Griggs, D.W.1    Johnston, M.2
  • 12
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller MM, Finger A, Schweiger M, Wolf DH (1996) ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273: 1725-1728
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 13
    • 0036173013 scopus 로고    scopus 로고
    • Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
    • Jarosch E et al (2002) Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol 4: 134-139
    • (2002) Nat. Cell Biol. , vol.4 , pp. 134-139
    • Jarosch, E.1
  • 14
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson ES, Ma PC, Ota IM, Varshavsky A (1995) A proteolytic pathway that recognizes ubiquitin as a degradation signal. J Biol Chem 270: 17442-17456
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 15
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito RR (2000) Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 10: 524-530
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 16
    • 0037566901 scopus 로고    scopus 로고
    • For whom the bell tolls: Protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection
    • Kostova Z, Wolf DH (2003) For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. EMBO J 22: 2309-2317
    • (2003) EMBO J. , vol.22 , pp. 2309-2317
    • Kostova, Z.1    Wolf, D.H.2
  • 17
    • 0037129213 scopus 로고    scopus 로고
    • A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
    • Lam YA, Lawson TG, Velayutham M, Zweier JL, Pickart C (2002) A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal. Nature 416: 763-767
    • (2002) Nature , vol.416 , pp. 763-767
    • Lam, Y.A.1    Lawson, T.G.2    Velayutham, M.3    Zweier, J.L.4    Pickart, C.5
  • 18
    • 0034671938 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis of a short-lived regulatory protein depends on its cellular localization
    • Lenk U, Sommer T (2000) Ubiquitin-mediated proteolysis of a short-lived regulatory protein depends on its cellular localization. J Biol Chem 275: 39403-39410
    • (2000) J. Biol. Chem. , vol.275 , pp. 39403-39410
    • Lenk, U.1    Sommer, T.2
  • 19
    • 0037646406 scopus 로고    scopus 로고
    • Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains
    • Raasi S, Pickart CM (2003) Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains. J Biol Chem 278: 8951-8959
    • (2003) J. Biol. Chem. , vol.278 , pp. 8951-8959
    • Raasi, S.1    Pickart, C.M.2
  • 20
    • 0037023716 scopus 로고    scopus 로고
    • Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23
    • Rao H, Sastry A (2002) Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23. J Biol Chem 277: 11691-11695
    • (2002) J. Biol. Chem. , vol.277 , pp. 11691-11695
    • Rao, H.1    Sastry, A.2
  • 21
    • 0035877846 scopus 로고    scopus 로고
    • Rad23 provides a link between the Png1 deglycosylating enzyme and the 26S proteasome in yeast
    • Suzuki T, Park H, Kwofie MA, Lennarz W (2001) Rad23 provides a link between the Png1 deglycosylating enzyme and the 26S proteasome in yeast. J Biol Chem 276: 21601-21607
    • (2001) J. Biol. Chem. , vol.276 , pp. 21601-21607
    • Suzuki, T.1    Park, H.2    Kwofie, M.A.3    Lennarz, W.4
  • 22
    • 0141592584 scopus 로고    scopus 로고
    • Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD
    • Taxis C, Hitt R, Park SH, Deak PM, Kostova Z, Wolf DH (2003) Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD. J Biol Chem 278: 35903-35913
    • (2003) J. Biol. Chem. , vol.278 , pp. 35903-35913
    • Taxis, C.1    Hitt, R.2    Park, S.H.3    Deak, P.M.4    Kostova, Z.5    Wolf, D.H.6
  • 23
    • 0035985150 scopus 로고    scopus 로고
    • ER-Golgi traffic is a prerequisite for efficient ER degradation
    • Taxis C, Vogel F, Wolf DH (2002) ER-Golgi traffic is a prerequisite for efficient ER degradation. Mol Biol Cell 13: 1806-1818
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1806-1818
    • Taxis, C.1    Vogel, F.2    Wolf, D.H.3
  • 24
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers KJ, Patil CK, Wodicka L, Lockhart DJ, Weissman JS, Walter P (2000) Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101: 249-258
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 25
    • 0029806477 scopus 로고    scopus 로고
    • The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover
    • van Nocker S et al (1996) The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol Cell Biol 16: 6020-6028
    • (1996) Mol. Cell Biol. , vol.16 , pp. 6020-6028
    • van Nocker, S.1
  • 26
    • 0027367944 scopus 로고
    • The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function
    • Watkins JF, Sung P, Prakash L, Prakash S (1993) The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function. Mol Cell Biol 13: 7757-7765
    • (1993) Mol. Cell Biol. , vol.13 , pp. 7757-7765
    • Watkins, J.F.1    Sung, P.2    Prakash, L.3    Prakash, S.4
  • 27
    • 0034798985 scopus 로고    scopus 로고
    • Proteins containing the UBA domain are able to bind to multi-ubiquitin chains
    • Wilkinson CR et al (2001) Proteins containing the UBA domain are able to bind to multi-ubiquitin chains. Nat Cell Biol 3: 939-943
    • (2001) Nat. Cell Biol. , vol.3 , pp. 939-943
    • Wilkinson, C.R.1
  • 28
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye Y, Meyer HH, Rapoport TA (2001) The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414: 652-656
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.