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Volumn 277, Issue 3, 2010, Pages 796-816

Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysis

Author keywords

RPN10; RPN13; Ubiquitin receptor; Ubiquitin recognition; UBL UBA factors

Indexed keywords

DNA 26S; PROTEASOME; UBIQUITIN;

EID: 75149172775     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2009.07531.x     Document Type: Article
Times cited : (43)

References (42)
  • 2
    • 28944435024 scopus 로고    scopus 로고
    • Mechanism of lysine 48-linked ubiquitin-chain synthesis by the Cullin-RING ubiquitin-ligase complex SCF-Cdc34
    • Petroski MD Deshaies RJ (2005) Mechanism of lysine 48-linked ubiquitin-chain synthesis by the Cullin-RING ubiquitin-ligase complex SCF-Cdc34. Cell 123, 1107 1120.
    • (2005) Cell , vol.123 , pp. 1107-1120
    • Petroski, M.D.1    Deshaies, R.J.2
  • 3
    • 50149086108 scopus 로고    scopus 로고
    • Diversity of degradation signals in the ubiquitin-proteasome system
    • Ravid T Hochstrasser M (2008) Diversity of degradation signals in the ubiquitin-proteasome system. Nat Rev Mol Cell Biol 9, 679 690.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 679-690
    • Ravid, T.1    Hochstrasser, M.2
  • 4
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • Verma R, Oania R, Graumann J Deshaies RJ (2004) Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell 118, 99 110.
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 6
    • 0034602845 scopus 로고    scopus 로고
    • Recognition of the polyubiquitin proteolytic signal
    • Thrower J, Hoffman L, Rechsteiner M Pickart C (2000) Recognition of the polyubiquitin proteolytic signal. EMBO J 19, 94 102.
    • (2000) EMBO J , vol.19 , pp. 94-102
    • Thrower, J.1    Hoffman, L.2    Rechsteiner, M.3    Pickart, C.4
  • 7
    • 0030052841 scopus 로고    scopus 로고
    • Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting
    • Beal R, Deveraux Q, Xia G, Rechsteiner M Pickart C (1996) Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting. Proc Natl Acad Sci USA 93, 861 866.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 861-866
    • Beal, R.1    Deveraux, Q.2    Xia, G.3    Rechsteiner, M.4    Pickart, C.5
  • 8
    • 43049162227 scopus 로고    scopus 로고
    • Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex
    • Jin L, Williamson A, Banerjee S, Philipp I Rape M (2008) Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex. Cell 133, 653 665.
    • (2008) Cell , vol.133 , pp. 653-665
    • Jin, L.1    Williamson, A.2    Banerjee, S.3    Philipp, I.4    Rape, M.5
  • 9
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson ES, Ma PCM, 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.M.2    Ota, I.M.3    Varshavsky, A.4
  • 10
    • 0035958926 scopus 로고    scopus 로고
    • In vitro assembly and recognition of Lys-63 polyubiquitin chains
    • Hofmann RM Pickart CM (2001) In vitro assembly and recognition of Lys-63 polyubiquitin chains. J Biol Chem 276, 27936 27943.
    • (2001) J Biol Chem , vol.276 , pp. 27936-27943
    • Hofmann, R.M.1    Pickart, C.M.2
  • 11
    • 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, Sadis S, Rubin D, Glickman M, Fu H, Coux O, Wefes I, Finley D Vierstra R (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    Sadis, S.2    Rubin, D.3    Glickman, M.4    Fu, H.5    Coux, O.6    Wefes, I.7    Finley, D.8    Vierstra, R.9
  • 14
    • 0037129213 scopus 로고    scopus 로고
    • A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
    • Lam YA, Lawson TG, Velayutham M, Zweier JL Pickart CM (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.M.5
  • 15
    • 0036382885 scopus 로고    scopus 로고
    • Identification of ubiquitin-like protein-binding subunits of the 26S proteasome
    • Saeki Y, Sone T, Toh-e A Yokosawa H (2002) Identification of ubiquitin-like protein-binding subunits of the 26S proteasome. Biochem Biophys Res Commun 296, 813 819.
    • (2002) Biochem Biophys Res Commun , vol.296 , pp. 813-819
    • Saeki, Y.1    Sone, T.2    Toh-E, A.3    Yokosawa, H.4
  • 16
    • 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
  • 17
    • 20444417275 scopus 로고    scopus 로고
    • The DNA damage-inducible UbL-UbA protein Ddi1 participates in Mec1-mediated degradation of Ho endonuclease
    • Kaplun L, Tzirkin R, Bakhrat A, Shabek N, Ivantsiv Y Raveh D (2005) The DNA damage-inducible UbL-UbA protein Ddi1 participates in Mec1-mediated degradation of Ho endonuclease. Mol Cell Biol 25, 5355 5362.
    • (2005) Mol Cell Biol , vol.25 , pp. 5355-5362
    • Kaplun, L.1    Tzirkin, R.2    Bakhrat, A.3    Shabek, N.4    Ivantsiv, Y.5    Raveh, D.6
  • 19
    • 23144449583 scopus 로고    scopus 로고
    • Delivery of ubiquitinated substrates to protein-unfolding machines
    • Elsasser S Finley D (2005) Delivery of ubiquitinated substrates to protein-unfolding machines. Nat Cell Biol 7, 742 749.
    • (2005) Nat Cell Biol , vol.7 , pp. 742-749
    • Elsasser, S.1    Finley, D.2
  • 20
    • 36249022073 scopus 로고    scopus 로고
    • Ubiquitin receptors and ERAD: A network of pathways to the proteasome
    • Raasi S Wolf DH (2007) Ubiquitin receptors and ERAD: a network of pathways to the proteasome. Semin Cell Dev Biol 18, 780 791.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 780-791
    • Raasi, S.1    Wolf, D.H.2
  • 22
    • 33750555919 scopus 로고    scopus 로고
    • Ubiquitin-binding domains
    • Hurley J, Lee S Prag G (2006) Ubiquitin-binding domains. Biochem J 399, 361 372.
    • (2006) Biochem J , vol.399 , pp. 361-372
    • Hurley, J.1    Lee, S.2    Prag, G.3
  • 25
    • 21744460209 scopus 로고    scopus 로고
    • Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites
    • Park S, Isaacson R, Kim HT, Silver PA Wagner G (2005) Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Structure 13, 995 1005.
    • (2005) Structure , vol.13 , pp. 995-1005
    • Park, S.1    Isaacson, R.2    Kim, H.T.3    Silver, P.A.4    Wagner, G.5
  • 26
    • 26944465404 scopus 로고    scopus 로고
    • Diverse polyubiquitin interaction properties of ubiquitin-associated domains
    • Raasi S, Varadan R, Fushman D Pickart CM (2005) Diverse polyubiquitin interaction properties of ubiquitin-associated domains. Nat Struct Mol Biol 12, 708 714.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 708-714
    • Raasi, S.1    Varadan, R.2    Fushman, D.3    Pickart, C.M.4
  • 27
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke L Dunn R (2003) Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu Rev Cell Dev Biol 19, 141 172.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 29
    • 21244459558 scopus 로고    scopus 로고
    • Ubiquitin binding site of the ubiquitin E2 variant (UEV) protein Mms2 is required for DNA damage tolerance in the yeast RAD6 pathway
    • Tsui C, Raguraj A Pickart CM (2005) Ubiquitin binding site of the ubiquitin E2 variant (UEV) protein Mms2 is required for DNA damage tolerance in the yeast RAD6 pathway. J Biol Chem 280, 19829 19835.
    • (2005) J Biol Chem , vol.280 , pp. 19829-19835
    • Tsui, C.1    Raguraj, A.2    Pickart, C.M.3
  • 30
    • 0031890210 scopus 로고    scopus 로고
    • Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26S proteasome subunit Mcb1
    • Fu H, Sadis S, Rubin DM, Glickman M, van Nocker S, Finley D Vierstra RD (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    Sadis, S.2    Rubin, D.M.3    Glickman, M.4    Van Nocker, S.5    Finley, D.6    Vierstra, R.D.7
  • 31
    • 0032489524 scopus 로고    scopus 로고
    • Characterization of two polyubiquitin binding sites in the 26S protease subunit 5a
    • Young P, Deveraux Q, Beal RE, Pickart CM Rechsteiner M (1998) Characterization of two polyubiquitin binding sites in the 26S protease subunit 5a. J Biol Chem 273, 5461 5467.
    • (1998) J Biol Chem , vol.273 , pp. 5461-5467
    • Young, P.1    Deveraux, Q.2    Beal, R.E.3    Pickart, C.M.4    Rechsteiner, M.5
  • 32
    • 0037390990 scopus 로고    scopus 로고
    • The pleiotropic role of the 26S proteasome subunit RPN10 in Arabidopsis growth and development supports a substrate-specific function in abscisic acid signaling
    • Smalle J, Kurepa J, Yang P, Emborg TJ, Babiychuk E, Kushnir S Vierstra RD (2003) The pleiotropic role of the 26S proteasome subunit RPN10 in Arabidopsis growth and development supports a substrate-specific function in abscisic acid signaling. Plant Cell 15, 965 980.
    • (2003) Plant Cell , vol.15 , pp. 965-980
    • Smalle, J.1    Kurepa, J.2    Yang, P.3    Emborg, T.J.4    Babiychuk, E.5    Kushnir, S.6    Vierstra, R.D.7
  • 33
    • 0031004447 scopus 로고    scopus 로고
    • Activities of CaMV 35S and nos promoters in pollen: Implications for field release of transgenic plants
    • Wilkinson JE, Twell D Lindsey K (1997) Activities of CaMV 35S and nos promoters in pollen: implications for field release of transgenic plants. J Exp Bot 48, 265 275.
    • (1997) J Exp Bot , vol.48 , pp. 265-275
    • Wilkinson, J.E.1    Twell, D.2    Lindsey, K.3
  • 34
    • 0037444494 scopus 로고    scopus 로고
    • Deletion of proteasomal subunit S5a/Rpn10/p54 causes lethality, multiple mitotic defects and overexpression of proteasomal genes in Drosophila melanogaster
    • Szlanka T, Haracska L, Kiss I, Deak P, Kurucz E, Ando I, Viragh E Udvardy A (2003) Deletion of proteasomal subunit S5a/Rpn10/p54 causes lethality, multiple mitotic defects and overexpression of proteasomal genes in Drosophila melanogaster. J Cell Sci 116, 1023 1033.
    • (2003) J Cell Sci , vol.116 , pp. 1023-1033
    • Szlanka, T.1    Haracska, L.2    Kiss, I.3    Deak, P.4    Kurucz, E.5    Ando, I.6    Viragh, E.7    Udvardy, A.8
  • 35
    • 34748859663 scopus 로고    scopus 로고
    • Rpn10-mediated degradation of ubiquitinated proteins is essential for mouse development
    • Hamazaki J, Sasaki K, Kawahara H, Hisanaga S-i, Tanaka K Murata S (2007) Rpn10-mediated degradation of ubiquitinated proteins is essential for mouse development. Mol Cell Biol 27, 6629 6638.
    • (2007) Mol Cell Biol , vol.27 , pp. 6629-6638
    • Hamazaki, J.1    Sasaki, K.2    Kawahara, H.3    S-I, H.4    Tanaka, K.5    Murata, S.6
  • 36
    • 0033177869 scopus 로고    scopus 로고
    • Multiubiquitin chain binding subunit MCB1 (RPN10) of the 26S proteasome is essential for developmental progression in Physcomitrella patens
    • Girod P, Fu H, Zryd J Vierstra R (1999) Multiubiquitin chain binding subunit MCB1 (RPN10) of the 26S proteasome is essential for developmental progression in Physcomitrella patens. Plant Cell 11, 1457 1472.
    • (1999) Plant Cell , vol.11 , pp. 1457-1472
    • Girod, P.1    Fu, H.2    Zryd, J.3    Vierstra, R.4
  • 37
    • 33845448653 scopus 로고    scopus 로고
    • Proteasomal ubiquitin receptor RPN-10 controls sex determination in Caenorhabditis elegans
    • Shimada M, Kanematsu K, Tanaka K, Yokosawa H Kawahara H (2006) Proteasomal ubiquitin receptor RPN-10 controls sex determination in Caenorhabditis elegans. Mol Biol Cell 17, 5356 5371.
    • (2006) Mol Biol Cell , vol.17 , pp. 5356-5371
    • Shimada, M.1    Kanematsu, K.2    Tanaka, K.3    Yokosawa, H.4    Kawahara, H.5
  • 38
    • 0037126632 scopus 로고    scopus 로고
    • Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome
    • Fu H, Reis N, Lee Y, Glickman M Vierstra R (2001) Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome. EMBO J 20, 7096 7107.
    • (2001) EMBO J , vol.20 , pp. 7096-7107
    • Fu, H.1    Reis, N.2    Lee, Y.3    Glickman, M.4    Vierstra, R.5
  • 40
    • 0342444416 scopus 로고
    • GUS fusions: Beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson R, Kavanagh T Bevan M (1987) GUS fusions: beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J 6, 3901 3907.
    • (1987) EMBO J , vol.6 , pp. 3901-3907
    • Jefferson, R.1    Kavanagh, T.2    Bevan, M.3
  • 41
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough SJ Bent AF (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J 16, 735 743.
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 42
    • 0004295111 scopus 로고    scopus 로고
    • How to isolate a gene defined by a mutation
    • Weigel, D. Glazebrook, J. eds. pp. Cold Spring Harbour Laboratory Press. Cold Spring Harbour, NY
    • Weigel D Glazebrook J (2002) How to isolate a gene defined by a mutation. In Arabidopsis: A Laboratory Manual (Weigel D Glazebrook J eds pp 168 169. Cold Spring Harbour Laboratory Press, Cold Spring Harbour, NY.
    • (2002) Arabidopsis: A Laboratory Manual , pp. 168-169
    • Weigel, D.1    Glazebrook, J.2


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