RSP5/YER125W Literature Guide Help

Other names published for RSP5: MDP1, MUT2, NPI1, UBY1, SMM1, NEDD4 family E3 ubiquitin-protein ligase, YER125W

RSP5 - Non-Fungal Related Genes/Proteins (26)

ReferenceOther Genes Addressed
Montanini B, et al.  (2011) Genome-wide search and functional identification of transcription factors in the mycorrhizal fungus Tuber melanosporum. New Phytol 189(3):736-50
Tofaris GK, et al.  (2011) Ubiquitin ligase Nedd4 promotes alpha-synuclein degradation by the endosomal-lysosomal pathway. Proc Natl Acad Sci U S A 108(41):17004-9
Liu F and Walters KJ  (2010) Multitasking with ubiquitin through multivalent interactions. Trends Biochem Sci 35(6):352-60
Yang B and Kumar S  (2010) Nedd4 and Nedd4-2: closely related ubiquitin-protein ligases with distinct physiological functions. Cell Death Differ 17(1):68-77
French ME, et al.  (2009) Regulation of the RSP5 Ubiquitin Ligase by an Intrinsic Ubiquitin-binding Site. J Biol Chem 284(18):12071-9
Lee JR, et al.  (2009) The HECT domain of the ubiquitin ligase Rsp5 contributes to substrate recognition. J Biol Chem 284(46):32126-37
Rotin D and Kumar S  (2009) Physiological functions of the HECT family of ubiquitin ligases. Nat Rev Mol Cell Biol 10(6):398-409
Alvarez CE  (2008) On the origins of arrestin and rhodopsin. BMC Evol Biol 8:222
Dehring DA, et al.  (2008) A C-terminal Sequence in the Guanine Nucleotide Exchange Factor Sec7 Mediates Golgi Association and Interaction with the Rsp5 Ubiquitin Ligase. J Biol Chem 283(49):34188-96
Nikko E and Andre B  (2007) Split-Ubiquitin Two-Hybrid Assay To Analyze Protein-Protein Interactions at the Endosome: Application to Saccharomyces cerevisiae Bro1 Interacting with ESCRT Complexes, the Doa4 Ubiquitin Hydrolase, and the Rsp5 Ubiquitin Ligase. Eukaryot Cell 6(8):1266-77
Kikkert M, et al.  (2005) The role of the ubiquitination machinery in dislocation and degradation of endoplasmic reticulum proteins. Curr Top Microbiol Immunol 300():57-93
Ingham RJ, et al.  (2004) The Nedd4 family of E3 ubiquitin ligases: functional diversity within a common modular architecture. Oncogene 23(11):1972-84
Salvat C, et al.  (2004) The -4 phenylalanine is required for substrate ubiquitination catalyzed by HECT ubiquitin ligases. J Biol Chem 279(18):18935-43
Gajewska B, et al.  (2003) Functional analysis of the human orthologue of the RSP5-encoded ubiquitin protein ligase, hNedd4, in yeast. Curr Genet 43(1):1-10
Zhong R and Ye ZH  (2003) The SAC domain-containing protein gene family in Arabidopsis. Plant Physiol 132(2):544-55
Shcherbik N, et al.  (2002) Substrate proteolysis is inhibited by dominant-negative Nedd4 and Rsp5 mutants harboring alterations in WW domain 1. J Cell Sci 115(Pt 5):1041-8
Harty RN, et al.  (2001) Rhabdoviruses and the cellular ubiquitin-proteasome system: a budding interaction. J Virol 75(22):10623-9
Kasanov J, et al.  (2001) Characterizing Class I WW domains defines key specificity determinants and generates mutant domains with novel specificities. Chem Biol 8(3):231-41
Rotin D, et al.  (2000) Ubiquitination and endocytosis of plasma membrane proteins: role of Nedd4/Rsp5p family of ubiquitin-protein ligases. J Membr Biol 176(1):1-17
Beaudenon SL, et al.  (1999) Rsp5 ubiquitin-protein ligase mediates DNA damage-induced degradation of the large subunit of RNA polymerase II in Saccharomyces cerevisiae. Mol Cell Biol 19(10):6972-9
Nuber U and Scheffner M  (1999) Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction. J Biol Chem 274(11):7576-82
Schwarz SE, et al.  (1998) Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7. J Biol Chem 273(20):12148-54
Imhof MO and McDonnell DP  (1996) Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent activation of transcription by human progesterone and glucocorticoid receptors. Mol Cell Biol 16(6):2594-605
Hofmann K and Bucher P  (1995) The rsp5-domain is shared by proteins of diverse functions. FEBS Lett 358(2):153-7
Huibregtse JM, et al.  (1995) A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc Natl Acad Sci U S A 92(7):2563-7
Andre B and Springael JY  (1994) WWP, a new amino acid motif present in single or multiple copies in various proteins including dystrophin and the SH3-binding Yes-associated protein YAP65. Biochem Biophys Res Commun 205(2):1201-5