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

作者: Antony S. Fatimababy , Ya-Ling Lin , Raju Usharani , Ramalingam Radjacommare , Hsing-Ting Wang

DOI: 10.1111/J.1742-4658.2009.07531.X

关键词:

摘要: The recognition of ubiquitylated substrates is an essential element ubiquitin/26S proteasome-mediated proteolysis (UPP), which mediated directly by the proteasome subunit RPN10 and/or RPN13, or indirectly ubiquitin receptors containing ubiquitin-like and ubiquitin-associated domains. By pull-down mutagenesis assays, we detected cross-species divergence major pathways. plays a role in direct Arabidopsis yeast based on strong affinity for long K48-linked chains. In contrast, both RPN13 homologs play roles humans. For indirect recognition, RAD23 DSK2 (except human homolog) are receptors. homolog targeted to 26S homologs. comparison, uses UIM1 UIM3 bind RAD23, respectively. Yeast UIM LRR RPN1. Overall, multiple subunits responsible single subunit, RPN10, critical pathways Arabidopsis. agreement with these results, accumulation severe pleiotropic phenotypes vegetative reproductive growth associated loss function T-DNA insertion mutant. This implies that targeting regulators involved affected. These results support mechanistic functional UPP.

参考文章(41)
R. A. Jefferson, T. A. Kavanagh, M. W. Bevan, GUS fusions: beta‐glucuronidase as a sensitive and versatile gene fusion marker in higher plants. The EMBO Journal. ,vol. 6, pp. 3901- 3907 ,(1987) , 10.1002/J.1460-2075.1987.TB02730.X
Hongyong Fu, Noa Reis, Yenfen Lee, Michael H Glickman, Richard D Vierstra, Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome The EMBO Journal. ,vol. 20, pp. 7096- 7107 ,(2001) , 10.1093/EMBOJ/20.24.7096
Masumi Shimada, Kenji Kanematsu, Keiji Tanaka, Hideyoshi Yokosawa, Hiroyuki Kawahara, Proteasomal Ubiquitin Receptor RPN-10 Controls Sex Determination in Caenorhabditis elegans Molecular Biology of the Cell. ,vol. 17, pp. 5356- 5371 ,(2006) , 10.1091/MBC.E06-05-0437
Hongyong Fu, Seth Sadis, David M. Rubin, Michael Glickman, Steven van Nocker, Daniel Finley, Richard D. Vierstra, Multiubiquitin Chain Binding and Protein Degradation Are Mediated by Distinct Domains within the 26 S Proteasome Subunit Mcb1 Journal of Biological Chemistry. ,vol. 273, pp. 1970- 1981 ,(1998) , 10.1074/JBC.273.4.1970
Tamás Szlanka, Lajos Haracska, István Kiss, Péter Deák, Éva Kurucz, István Andó, Erika Virágh, Andor Udvardy, Deletion of proteasomal subunit S5a/Rpn10/p54 causes lethality, multiple mitotic defects and overexpression of proteasomal genes in Drosophila melanogaster Journal of Cell Science. ,vol. 116, pp. 1023- 1033 ,(2003) , 10.1242/JCS.00332
Erica S. Johnson, Philip C. M. Ma, Irene M. Ota, Alexander Varshavsky, A proteolytic pathway that recognizes ubiquitin as a degradation signal. Journal of Biological Chemistry. ,vol. 270, pp. 17442- 17456 ,(1995) , 10.1074/JBC.270.29.17442
Atsuhiro Kanayama, Rashu B. Seth, Lijun Sun, Chee-Kwee Ea, Mei Hong, Abdullah Shaito, Yu-Hsin Chiu, Li Deng, Zhijian J. Chen, TAB2 and TAB3 Activate the NF-κB Pathway through Binding to Polyubiquitin Chains Molecular Cell. ,vol. 15, pp. 535- 548 ,(2004) , 10.1016/J.MOLCEL.2004.08.008
Y. Amy Lam, T. Glen Lawson, Murugesan Velayutham, Jay L. Zweier, Cecile M. Pickart, A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal Nature. ,vol. 416, pp. 763- 767 ,(2002) , 10.1038/416763A
Sunghyouk Park, Rivka Isaacson, Hyoung Tae Kim, Pamela A. Silver, Gerhard Wagner, Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Structure. ,vol. 13, pp. 995- 1005 ,(2005) , 10.1016/J.STR.2005.04.013
Xuemei Yuan, Peter Simpson, Ciaran Mckeown, Hisao Kondo, Keiji Uchiyama, Russell Wallis, Ingrid Dreveny, Catherine Keetch, Xiaodong Zhang, Carol Robinson, Paul Freemont, Stephen Matthews, Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97 The EMBO Journal. ,vol. 23, pp. 1463- 1473 ,(2004) , 10.1038/SJ.EMBOJ.7600152