RPN10/YHR200W Literature Guide Help

Other names published for RPN10: MCB1, SUN1, proteasome regulatory particle base subunit RPN10, YHR200W

RPN10 - Substrates/Ligands/Cofactors (19)

ReferenceOther Genes Addressed
Ha SW, et al.  (2012) The N-terminal domain of Rpn4 serves as a portable ubiquitin-independent degron and is recognized by specific 19S RP subunits. Biochem Biophys Res Commun 419(2):226-31
Sakata E, et al.  (2012) Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy. Proc Natl Acad Sci U S A 109(5):1479-84
Henderson A, et al.  (2011) Dependence of proteasome processing rate on substrate unfolding. J Biol Chem 286(20):17495-502
Kraut DA and Matouschek A  (2011) Proteasomal degradation from internal sites favors partial proteolysis via remote domain stabilization. ACS Chem Biol 6(10):1087-95
Fatimababy AS, et al.  (2010) Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysis. FEBS J 277(3):796-816
Peth A, et al.  (2010) ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation. Mol Cell 40(4):671-81
Prakash S, et al.  (2009) Substrate selection by the proteasome during degradation of protein complexes. Nat Chem Biol 5(1):29-36
Zhang D, et al.  (2009) Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor. Mol Cell 36(6):1018-33
Seong KM, et al.  (2007) Rpn10p is a receptor for ubiquitinated Gcn4p in proteasomal proteolysis. Mol Cells 24(2):194-9
Seong KM, et al.  (2007) Rpn13p and Rpn14p are involved in the recognition of ubiquitinated Gcn4p by the 26S proteasome. FEBS Lett 581(13):2567-73
Mayor T, et al.  (2005) Analysis of polyubiquitin conjugates reveals that the Rpn10 substrate receptor contributes to the turnover of multiple proteasome targets. Mol Cell Proteomics 4(6):741-51
Gaczynska M, et al.  (2003) Proline- and arginine-rich peptides constitute a novel class of allosteric inhibitors of proteasome activity. Biochemistry 42(29):8663-70
Heessen S, et al.  (2003) Inhibition of ubiquitin/proteasome-dependent proteolysis in Saccharomyces cerevisiae by a Gly-Ala repeat. FEBS Lett 555(2):397-404
Saeki Y, et al.  (2002) Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis. Biochem Biophys Res Commun 293(3):986-92
Loidl G, et al.  (1999) Bivalency as a principle for proteasome inhibition. Proc Natl Acad Sci U S A 96(10):5418-22
Fu H, et al.  (1998) Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1. J Biol Chem 273(4):1970-81
Glickman MH, et al.  (1998) A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell 94(5):615-23
Rubin DM, et al.  (1997) ATPase and ubiquitin-binding proteins of the yeast proteasome. Mol Biol Rep 24(1-2):17-26
Fischer M, et al.  (1994) The 26S proteasome of the yeast Saccharomyces cerevisiae. FEBS Lett 355(1):69-75