| http://purl.uniprot.org/citations/16840785 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16840785 | http://www.w3.org/2000/01/rdf-schema#comment | "Small heat shock proteins (sHsps) exist in dynamic oligomeric complexes and display diverse biological functions ranging from chaperone properties to modulator of apoptosis. So far, the role of stress-dependent phosphorylation of mammalian sHsps for its structure and function has been analyzed by using various phosphorylation site mutants overexpressed in different cell types as well as by non-exclusive inhibitors of the p38 MAPK cascade. Here we investigate the role of phosphorylation of endogenous sHsp in a genetic model lacking the major Hsp25 kinase, the MAP kinase-activated protein kinase MK2. We demonstrate that in MK2-deficient fibroblasts, where no stress-dependent phosphorylation of Hsp25 at Ser86 and no in vitro binding to 14-3-3 was detectable, stress-dependent disaggregation of endogenous Hsp25 complexes is impared and kinetics of arsenite-dependent, H2O2-dependent, and sublethal heat shock-induced insolubilization of Hsp25 is delayed. Similarly, green fluorescent protein-tagged Hsp25 shows retarded subcellular accumulation into stress granules in MK2-deficient cells after arsenite treatment. Decreased insolubilization of Hsp25 in MK2-deficient cells correlates with increased resistance against arsenite, H2O2, and sublethal heat shock treatment and with decreased apoptosis. In contrast, after severe, lethal heat shock MK2-deficient embryonic fibroblasts cells show fast and complete insolubilization of Hsp25 independent of MK2 and no increased stress resistance. Hence, MK2-dependent formation of insoluble stress granules and irreversible cell damage by oxidative stresses and sublethal heat shock correlate and only upon severe, lethal heat shock MK2-independent processes could determine insolubilization of Hsp25 and are more relevant for cellular stress damage."xsd:string |
| http://purl.uniprot.org/citations/16840785 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m602134200"xsd:string |
| http://purl.uniprot.org/citations/16840785 | http://purl.uniprot.org/core/author | "Gaestel M."xsd:string |
| http://purl.uniprot.org/citations/16840785 | http://purl.uniprot.org/core/author | "Hakim C."xsd:string |
| http://purl.uniprot.org/citations/16840785 | http://purl.uniprot.org/core/author | "Kotlyarov A."xsd:string |
| http://purl.uniprot.org/citations/16840785 | http://purl.uniprot.org/core/author | "Vertii A."xsd:string |
| http://purl.uniprot.org/citations/16840785 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16840785 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/16840785 | http://purl.uniprot.org/core/pages | "26966-26975"xsd:string |
| http://purl.uniprot.org/citations/16840785 | http://purl.uniprot.org/core/title | "Analysis of properties of small heat shock protein Hsp25 in MAPK-activated protein kinase 2 (MK2)-deficient cells: MK2-dependent insolubilization of Hsp25 oligomers correlates with susceptibility to stress."xsd:string |
| http://purl.uniprot.org/citations/16840785 | http://purl.uniprot.org/core/volume | "281"xsd:string |
| http://purl.uniprot.org/citations/16840785 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16840785 |
| http://purl.uniprot.org/citations/16840785 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16840785 |
| http://purl.uniprot.org/uniprot/#_Q63932-mappedCitation-16840785 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16840785 |
| http://purl.uniprot.org/uniprot/#_Q3USU3-mappedCitation-16840785 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16840785 |
| http://purl.uniprot.org/uniprot/#_Q8CB46-mappedCitation-16840785 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16840785 |
| http://purl.uniprot.org/uniprot/#_P14602-mappedCitation-16840785 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16840785 |
| http://purl.uniprot.org/uniprot/#_P04792-mappedCitation-16840785 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16840785 |
| http://purl.uniprot.org/uniprot/#_Q3UPM3-mappedCitation-16840785 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16840785 |
| http://purl.uniprot.org/uniprot/#_Q545F4-mappedCitation-16840785 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16840785 |
| http://purl.uniprot.org/uniprot/#_Q9Z2L2-mappedCitation-16840785 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16840785 |
| http://purl.uniprot.org/uniprot/#_Q9Z2L3-mappedCitation-16840785 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16840785 |
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| http://purl.uniprot.org/uniprot/Q63932 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/16840785 |