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http://purl.uniprot.org/citations/15016827http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15016827http://www.w3.org/2000/01/rdf-schema#comment"Protein phosphatase-1 (PP1) catalytic subunit isoforms interact with diverse proteins, typically containing a canonical (R/K)(V/I)XF motif. Despite sharing approximately 90% amino acid sequence identity, PP1beta and PP1gamma1 have distinct subcellular localizations that may be determined by selective interactions with PP1-binding proteins. Immunoprecipitation studies from brain and muscle extracts demonstrated that PP1gamma1 selectively interacts with spinophilin and neurabin, F-actin-targeting proteins, whereas PP1beta selectively interacted with G(M)/R(GL), the striated-muscle glycogen-targeting subunit. Glutathione S-transferase (GST) fusion proteins containing residues 146-493 of neurabin (GST-Nb-(146-493)) or residues 1-240 of G(M)/R(GL) (GST-G(M)-(1-240)) recapitulated these isoform selectivities in binding and phosphatase activity inhibition assays. Site-directed mutagenesis indicated that this isoform selectivity was not due to sequence differences between the canonical PP1-binding motifs (neurabin, (457)KIKF(460); G(M)/R(GL), (65)RVSF(68)). A chimeric GST fusion protein containing residues 1-64 of G(M)/R(GL) fused to residues 457-493 of neurabin (GST-G(M)/Nb) selectively bound to and inhibited PP1gamma1, whereas a GST-Nb/G(M) chimera containing Nb-(146-460) fused to G(M)-(69-240) selectively interacted with and weakly inhibited PP1beta, implicating domain(s) C-terminal to the (R/K)(V/I)XF motif as determinants of PP1 isoform selectivity. Deletion of Pro(464) and Ile(465) in neurabin (deltaPI) to equally space a conserved cluster of amino acids from the (R/K)(V/I)XF motif as in G(M)/R(GL) severely compromised the ability of neurabin to bind and inhibit both isoforms but did not affect PP1gamma1 selectivity. Further analysis of a series of C-terminal truncated GST-Nb-(146-493) proteins identified residues 473-479 of neurabin as containing a crucial PP1gamma1-selectivity determinant. In combination, these data identify a novel PP1gamma1-selective interaction domain in neurabin that may allow for selective regulation and/or subcellular targeting of PP1 isoforms."xsd:string
http://purl.uniprot.org/citations/15016827http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m402261200"xsd:string
http://purl.uniprot.org/citations/15016827http://purl.uniprot.org/core/author"Colbran R.J."xsd:string
http://purl.uniprot.org/citations/15016827http://purl.uniprot.org/core/author"DePaoli-Roach A.A."xsd:string
http://purl.uniprot.org/citations/15016827http://purl.uniprot.org/core/author"Bass M.A."xsd:string
http://purl.uniprot.org/citations/15016827http://purl.uniprot.org/core/author"Carmody L.C."xsd:string
http://purl.uniprot.org/citations/15016827http://purl.uniprot.org/core/author"Bauman P.A."xsd:string
http://purl.uniprot.org/citations/15016827http://purl.uniprot.org/core/author"Mavila N."xsd:string
http://purl.uniprot.org/citations/15016827http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15016827http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/15016827http://purl.uniprot.org/core/pages"21714-21723"xsd:string
http://purl.uniprot.org/citations/15016827http://purl.uniprot.org/core/title"A protein phosphatase-1gamma1 isoform selectivity determinant in dendritic spine-associated neurabin."xsd:string
http://purl.uniprot.org/citations/15016827http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/15016827http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15016827
http://purl.uniprot.org/citations/15016827http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15016827
http://purl.uniprot.org/uniprot/#_A0A0G2JGC1-mappedCitation-15016827http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15016827
http://purl.uniprot.org/uniprot/#_A0A0G2JE42-mappedCitation-15016827http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15016827
http://purl.uniprot.org/uniprot/#_A0A0G2JEB0-mappedCitation-15016827http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15016827
http://purl.uniprot.org/uniprot/#_A0A0G2JF34-mappedCitation-15016827http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15016827
http://purl.uniprot.org/uniprot/#_P63087-mappedCitation-15016827http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15016827
http://purl.uniprot.org/uniprot/#_P63088-mappedCitation-15016827http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15016827
http://purl.uniprot.org/uniprot/#_A0A0G2JFF1-mappedCitation-15016827http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15016827
http://purl.uniprot.org/uniprot/#_A6IDS7-mappedCitation-15016827http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15016827
http://purl.uniprot.org/uniprot/#_A6IDS9-mappedCitation-15016827http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15016827