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000137502 0247_ $$2doi$$a10.1074/mcp.M113.035154
000137502 0247_ $$2pmid$$apmid:24925903
000137502 0247_ $$2pmc$$apmc:PMC4125733
000137502 0247_ $$2ISSN$$a1535-9476
000137502 0247_ $$2ISSN$$a1535-9484
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000137502 037__ $$aDZNE-2020-03824
000137502 041__ $$aEnglish
000137502 082__ $$a610
000137502 1001_ $$0P:(DE-HGF)0$$aCorradini, Eleonora$$b0
000137502 245__ $$aAlterations in the cerebellar (Phospho)proteome of a cyclic guanosine monophosphate (cGMP)-dependent protein kinase knockout mouse.
000137502 260__ $$aBethesda, Md.$$bThe American Society for Biochemistry and Molecular Biology$$c2014
000137502 264_1 $$2Crossref$$3online$$bAmerican Society for Biochemistry & Molecular Biology (ASBMB)$$c2014-06-12
000137502 264_1 $$2Crossref$$3print$$bAmerican Society for Biochemistry & Molecular Biology (ASBMB)$$c2014-08-01
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000137502 520__ $$aThe cyclic nucleotide cyclic guanosine monophosphate (cGMP) plays an important role in learning and memory, but its signaling mechanisms in the mammalian brain are not fully understood. Using mass-spectrometry-based proteomics, we evaluated how the cerebellum adapts its (phospho)proteome in a knockout mouse model of cGMP-dependent protein kinase type I (cGKI). Our data reveal that a small subset of proteins in the cerebellum (∼3% of the quantified proteins) became substantially differentially expressed in the absence of cGKI. More changes were observed at the phosphoproteome level, with hundreds of sites being differentially phosphorylated between wild-type and knockout cerebellum. Most of these phosphorylated sites do not represent known cGKI substrates. An integrative computational network analysis of the data indicated that the differentially expressed proteins and proteins harboring differentially phosphorylated sites largely belong to a tight network in the Purkinje cells of the cerebellum involving important cGMP/cAMP signaling nodes (e.g. PDE5 and PKARIIβ) and Ca(2+) signaling (e.g. SERCA3). In this way, removal of cGKI could be linked to impaired cerebellar long-term depression at Purkinje cell synapses. In addition, we were able to identify a set of novel putative (phospho)proteins to be considered in this network. Overall, our data improve our understanding of cerebellar cGKI signaling and suggest novel players in cGKI-regulated synaptic plasticity.
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000137502 650_7 $$2NLM Chemicals$$aPhosphoproteins
000137502 650_7 $$0EC 2.7.11.12$$2NLM Chemicals$$aCyclic GMP-Dependent Protein Kinase Type I
000137502 650_7 $$0EC 2.7.11.12$$2NLM Chemicals$$aPrkg1 protein, mouse
000137502 650_7 $$0H2D2X058MU$$2NLM Chemicals$$aCyclic GMP
000137502 650_2 $$2MeSH$$aAnimals
000137502 650_2 $$2MeSH$$aCerebellum: metabolism
000137502 650_2 $$2MeSH$$aCyclic GMP
000137502 650_2 $$2MeSH$$aCyclic GMP-Dependent Protein Kinase Type I: genetics
000137502 650_2 $$2MeSH$$aCyclic GMP-Dependent Protein Kinase Type I: metabolism
000137502 650_2 $$2MeSH$$aMice
000137502 650_2 $$2MeSH$$aMice, Knockout
000137502 650_2 $$2MeSH$$aPhosphoproteins: isolation & purification
000137502 650_2 $$2MeSH$$aPhosphorylation
000137502 650_2 $$2MeSH$$aProteomics: methods
000137502 650_2 $$2MeSH$$aSignal Transduction
000137502 650_2 $$2MeSH$$aSynapses: metabolism
000137502 7001_ $$0P:(DE-2719)2551172$$aVallur, Raghavan$$b1$$udzne
000137502 7001_ $$0P:(DE-HGF)0$$aRaaijmakers, Linsey M$$b2
000137502 7001_ $$0P:(DE-HGF)0$$aFeil, Susanne$$b3
000137502 7001_ $$0P:(DE-HGF)0$$aFeil, Robert$$b4
000137502 7001_ $$0P:(DE-HGF)0$$aHeck, Albert J R$$b5$$eCorresponding author
000137502 7001_ $$0P:(DE-HGF)0$$aScholten, Arjen$$b6
000137502 77318 $$2Crossref$$3journal-article$$a10.1074/mcp.m113.035154$$b : American Society for Biochemistry & Molecular Biology (ASBMB), 2014-06-12$$n8$$p2004-2016$$tMolecular & Cellular Proteomics$$v13$$x1535-9476$$y2014
000137502 773__ $$0PERI:(DE-600)2071375-7$$a10.1074/mcp.M113.035154$$gVol. 13, no. 8, p. 2004 - 2016$$n8$$p2004-2016$$q13:8<2004 - 2016$$tMolecular & cellular proteomics$$v13$$x1535-9476$$y2014
000137502 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC4125733
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000137502 9141_ $$y2014
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