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| Home > Publications Database > Alterations in the cerebellar (Phospho)proteome of a cyclic guanosine monophosphate (cGMP)-dependent protein kinase knockout mouse. > print |
| Home > Publications Database > Alterations in the cerebellar (Phospho)proteome of a cyclic guanosine monophosphate (cGMP)-dependent protein kinase knockout mouse. > print |
| 001 | 137502 | ||
| 005 | 20240321220248.0 | ||
| 024 | 7 | _ | |a 10.1074/mcp.M113.035154 |2 doi |
| 024 | 7 | _ | |a pmid:24925903 |2 pmid |
| 024 | 7 | _ | |a pmc:PMC4125733 |2 pmc |
| 024 | 7 | _ | |a 1535-9476 |2 ISSN |
| 024 | 7 | _ | |a 1535-9484 |2 ISSN |
| 024 | 7 | _ | |a altmetric:3894229 |2 altmetric |
| 037 | _ | _ | |a DZNE-2020-03824 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 610 |
| 100 | 1 | _ | |a Corradini, Eleonora |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Alterations in the cerebellar (Phospho)proteome of a cyclic guanosine monophosphate (cGMP)-dependent protein kinase knockout mouse. |
| 260 | _ | _ | |a Bethesda, Md. |c 2014 |b The American Society for Biochemistry and Molecular Biology |
| 264 | _ | 1 | |3 online |2 Crossref |b American Society for Biochemistry & Molecular Biology (ASBMB) |c 2014-06-12 |
| 264 | _ | 1 | |3 print |2 Crossref |b American Society for Biochemistry & Molecular Biology (ASBMB) |c 2014-08-01 |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1589204174_516 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a The 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. |
| 536 | _ | _ | |a 344 - Clinical and Health Care Research (POF3-344) |0 G:(DE-HGF)POF3-344 |c POF3-344 |f POF III |x 0 |
| 588 | _ | _ | |a Dataset connected to CrossRef, PubMed, |
| 650 | _ | 7 | |a Phosphoproteins |2 NLM Chemicals |
| 650 | _ | 7 | |a Cyclic GMP-Dependent Protein Kinase Type I |0 EC 2.7.11.12 |2 NLM Chemicals |
| 650 | _ | 7 | |a Prkg1 protein, mouse |0 EC 2.7.11.12 |2 NLM Chemicals |
| 650 | _ | 7 | |a Cyclic GMP |0 H2D2X058MU |2 NLM Chemicals |
| 650 | _ | 2 | |a Animals |2 MeSH |
| 650 | _ | 2 | |a Cerebellum: metabolism |2 MeSH |
| 650 | _ | 2 | |a Cyclic GMP |2 MeSH |
| 650 | _ | 2 | |a Cyclic GMP-Dependent Protein Kinase Type I: genetics |2 MeSH |
| 650 | _ | 2 | |a Cyclic GMP-Dependent Protein Kinase Type I: metabolism |2 MeSH |
| 650 | _ | 2 | |a Mice |2 MeSH |
| 650 | _ | 2 | |a Mice, Knockout |2 MeSH |
| 650 | _ | 2 | |a Phosphoproteins: isolation & purification |2 MeSH |
| 650 | _ | 2 | |a Phosphorylation |2 MeSH |
| 650 | _ | 2 | |a Proteomics: methods |2 MeSH |
| 650 | _ | 2 | |a Signal Transduction |2 MeSH |
| 650 | _ | 2 | |a Synapses: metabolism |2 MeSH |
| 700 | 1 | _ | |a Vallur, Raghavan |0 P:(DE-2719)2551172 |b 1 |u dzne |
| 700 | 1 | _ | |a Raaijmakers, Linsey M |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Feil, Susanne |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Feil, Robert |0 P:(DE-HGF)0 |b 4 |
| 700 | 1 | _ | |a Heck, Albert J R |0 P:(DE-HGF)0 |b 5 |e Corresponding author |
| 700 | 1 | _ | |a Scholten, Arjen |0 P:(DE-HGF)0 |b 6 |
| 773 | 1 | 8 | |a 10.1074/mcp.m113.035154 |b : American Society for Biochemistry & Molecular Biology (ASBMB), 2014-06-12 |n 8 |p 2004-2016 |3 journal-article |2 Crossref |t Molecular & Cellular Proteomics |v 13 |y 2014 |x 1535-9476 |
| 773 | _ | _ | |a 10.1074/mcp.M113.035154 |g Vol. 13, no. 8, p. 2004 - 2016 |0 PERI:(DE-600)2071375-7 |n 8 |q 13:8<2004 - 2016 |p 2004-2016 |t Molecular & cellular proteomics |v 13 |y 2014 |x 1535-9476 |
| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4125733 |
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