RPN1/YHR027C Literature Guide Help

Other names published for RPN1: HRD2, NAS1, proteasome regulatory particle base subunit RPN1, YHR027C

RPN1 - Strains/Constructs (30)

ReferenceOther Genes Addressed
Enenkel C  (2012) Using Native Gel Electrophoresis and Phosphofluoroimaging to Analyze GFP-Tagged Proteasomes. Methods Mol Biol 832():339-48
Rosenzweig R, et al.  (2012) Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome. J Biol Chem 287(18):14659-71
Franzosa EA, et al.  (2011) Heterozygous yeast deletion collection screens reveal essential targets of hsp90. PLoS One 6(11):e28211
Gomez TA, et al.  (2011) Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1. BMC Biol 9(1):33
Hatanaka A, et al.  (2011) Fub1p, a novel protein isolated by boundary screening, binds the proteasome complex. Genes Genet Syst 86(5):305-14
Sakata E, et al.  (2011) The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle. Mol Cell 42(5):637-49
Sekiguchi T, et al.  (2011) Ubiquitin chains in the Dsk2 UBL domain mediate Dsk2 stability and protein degradation in yeast. Biochem Biophys Res Commun 411(3):555-61
Wang Y, et al.  (2011) Ubiquitin-dependent Proteasomal Degradation of Human Liver Cytochrome P450 2E1: IDENTIFICATION OF SITES TARGETED FOR PHOSPHORYLATION AND UBIQUITINATION. J Biol Chem 286(11):9443-56
Chandra A, et al.  (2010) Proteasome assembly influences interaction with ubiquitinated proteins and shuttle factors. J Biol Chem 285(11):8330-9
Cortajarena AL, et al.  (2010) Designed proteins to modulate cellular networks. ACS Chem Biol 5(6):545-52
Effantin G, et al.  (2009) Electron Microscopic Evidence in Support of alpha-Solenoid Models of Proteasomal Subunits Rpn1 and Rpn2. J Mol Biol 386(5):1204-11
Garza RM, et al.  (2009) In vitro analysis of Hrd1p-mediated retrotranslocation of its multispanning membrane substrate 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase. J Biol Chem 284(22):14710-22
Le Tallec B, et al.  (2009) Hsm3/S5b participates in the assembly pathway of the 19S regulatory particle of the proteasome. Mol Cell 33(3):389-99
Park S, et al.  (2009) Hexameric assembly of the proteasomal ATPases is templated through their C termini. Nature 459(7248):866-70
Wu CY, et al.  (2009) Repression of sulfate assimilation is an adaptive response of yeast to the oxidative stress of zinc deficiency. J Biol Chem 284(40):27544-56
Guerrero C, et al.  (2008) Characterization of the proteasome interaction network using a QTAX-based tag-team strategy and protein interaction network analysis. Proc Natl Acad Sci U S A 105(36):13333-8
Laporte D, et al.  (2008) Reversible cytoplasmic localization of the proteasome in quiescent yeast cells. J Cell Biol 181(5):737-45
Ishii T, et al.  (2006) Yeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway. EMBO J 25(23):5492-503
Liao M, et al.  (2006) Endoplasmic reticulum-associated degradation of cytochrome P450 CYP3A4 in Saccharomyces cerevisiae: further characterization of cellular participants and structural determinants. Mol Pharmacol 69(6):1897-904
Lee D, et al.  (2005) The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators. Cell 123(3):423-36
Elsasser S, et al.  (2004) Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome. J Biol Chem 279(26):26817-22
Kim I, et al.  (2004) Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis. Mol Biol Cell 15(7):3357-65
Wendler P, et al.  (2004) The bipartite nuclear localization sequence of Rpn2 is required for nuclear import of proteasomal base complexes via karyopherin alphabeta and proteasome functions. J Biol Chem 279(36):37751-62
Imai J, et al.  (2003) The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. EMBO J 22(14):3557-67
Elsasser S, et al.  (2002) Proteasome subunit Rpn1 binds ubiquitin-like protein domains. Nat Cell Biol 4(9):725-30
Funakoshi M, et al.  (2002) Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc Natl Acad Sci U S A 99(2):745-50
Gardner RG, et al.  (2001) In vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation. Mol Cell Biol 21(13):4276-91
Murray BP and Correia MA  (2001) Ubiquitin-dependent 26S proteasomal pathway: a role in the degradation of native human liver CYP3A4 expressed in Saccharomyces cerevisiae? Arch Biochem Biophys 393(1):106-16
Loayza D, et al.  (1998) Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae. Mol Biol Cell 9(10):2767-84
Hampton RY, et al.  (1996) Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol Biol Cell 7(12):2029-44