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http://purl.uniprot.org/citations/20519502http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20519502http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20519502http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/20519502http://www.w3.org/2000/01/rdf-schema#comment"Tubulin polyglutamylation is a reversible post-translational modification, serving important roles in microtubule (MT)-related processes. Polyglutamylases of the tubulin tyrosine ligase-like (TTLL) family add glutamate moieties to specific tubulin glutamate residues, whereas as yet unknown deglutamylases shorten polyglutamate chains. First we investigated regulatory machinery of tubulin glutamylation in MT-based sensory cilia of the roundworm Caenorhabditis elegans. We found that ciliary MTs were polyglutamylated by a process requiring ttll-4. Conversely, loss of ccpp-6 gene function, which encodes one of two cytosolic carboxypeptidases (CCPs), resulted in elevated levels of ciliary MT polyglutamylation. Consistent with a deglutamylase function for ccpp-6, overexpression of this gene in ciliated cells decreased polyglutamylation signals. Similarly, we confirmed that overexpression of murine CCP5, one of two sequence orthologs of nematode ccpp-6, caused a dramatic loss of MT polyglutamylation in cultured mammalian cells. Finally, using an in vitro assay for tubulin glutamylation, we found that recombinantly expressed Myc-tagged CCP5 exhibited deglutamylase biochemical activities. Together, these data from two evolutionarily divergent systems identify C. elegans CCPP-6 and its mammalian ortholog CCP5 as a tubulin deglutamylase."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c110.128280"xsd:string
http://purl.uniprot.org/citations/20519502http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c110.128280"xsd:string
http://purl.uniprot.org/citations/20519502http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c110.128280"xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Kimura Y."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Kimura Y."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Tsutsumi K."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Tsutsumi K."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Ikegami K."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Ikegami K."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Iino Y."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Iino Y."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Kunitomo H."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Kunitomo H."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Blacque O.E."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Blacque O.E."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Kurabe N."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Kurabe N."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Setou M."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Setou M."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Kaplan O.I."xsd:string
http://purl.uniprot.org/citations/20519502http://purl.uniprot.org/core/author"Kaplan O.I."xsd:string