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http://purl.uniprot.org/citations/21454489http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21454489http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21454489http://www.w3.org/2000/01/rdf-schema#comment"Protein phosphatase 2A (PP2A) is regulated through a variety of mechanisms, including post-translational modifications and association with regulatory proteins. Alpha4 is one such regulatory protein that binds the PP2A catalytic subunit (PP2Ac) and protects it from polyubiquitination and degradation. Alpha4 is a multidomain protein with a C-terminal domain that binds Mid1, a putative E3 ubiquitin ligase, and an N-terminal domain containing the PP2Ac-binding site. In this work, we present the structure of the N-terminal domain of mammalian Alpha4 determined by x-ray crystallography and use double electron-electron resonance spectroscopy to show that it is a flexible tetratricopeptide repeat-like protein. Structurally, Alpha4 differs from its yeast homolog, Tap42, in two important ways: 1) the position of the helix containing the PP2Ac-binding residues is in a more open conformation, showing flexibility in this region; and 2) Alpha4 contains a ubiquitin-interacting motif. The effects of wild-type and mutant Alpha4 on PP2Ac ubiquitination and stability were examined in mammalian cells by performing tandem ubiquitin-binding entity precipitations and cycloheximide chase experiments. Our results reveal that both the C-terminal Mid1-binding domain and the PP2Ac-binding determinants are required for Alpha4-mediated protection of PP2Ac from polyubiquitination and degradation."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m111.222414"xsd:string
http://purl.uniprot.org/citations/21454489http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m111.222414"xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/author"Wadzinski B.E."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/author"Wadzinski B.E."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/author"Spiller B.W."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/author"Spiller B.W."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/author"Zou P."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/author"Zou P."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/author"Germane K.L."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/author"Germane K.L."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/author"LeNoue-Newton M."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/author"LeNoue-Newton M."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/author"McCorvey L.R."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/author"McCorvey L.R."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/author"Watkins G.R."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/author"Watkins G.R."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/pages"17665-17671"xsd:string
http://purl.uniprot.org/citations/21454489http://purl.uniprot.org/core/pages"17665-17671"xsd:string