| http://purl.uniprot.org/citations/22450169 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22450169 | http://www.w3.org/2000/01/rdf-schema#comment | "It has been previously reported that phosphorylated cofilin interacted with 14-3-3ζ protein to generate a sub-micromolar K(d) binary complex. Here we challenge this hypothesis by analyzing the direct association of recombinant cofilin with 14-3-3ζ using different in vitro biochemical methods. Phosphorylated cofilin at high concentration binds to 14-3-3 immobilized on nitrocellulose, however no complex formation was detected by means of native gel electrophoresis or chemical crosslinking. Intact dimeric or mutant monomeric 14-3-3 was unable to form stable complexes with phosphorylated or unphosphorylated cofilin detected by size-exclusion chromatography. In co-sedimentation assay 14-3-3 did not affect interaction of cofilin with F-actin. The data of native gel electrophoresis indicate that 14-3-3 did not affect interaction of cofilin with G-actin. Thus, cofilin only weakly interacts with 14-3-3 and therefore cannot directly compete with phosphorylated small heat shock protein HspB6 for its binding to 14-3-3. It is hypothesized that phosphorylated HspB6 might affect interaction of 14-3-3 with protein phosphatases (and/or protein kinases) involved in dephosphorylation (or phosphorylation) of cofilin and by this means regulate cofilin-dependent reorganization of cytoskeleton."xsd:string |
| http://purl.uniprot.org/citations/22450169 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.abb.2012.03.010"xsd:string |
| http://purl.uniprot.org/citations/22450169 | http://purl.uniprot.org/core/author | "Gusev N.B."xsd:string |
| http://purl.uniprot.org/citations/22450169 | http://purl.uniprot.org/core/author | "Seit-Nebi A.S."xsd:string |
| http://purl.uniprot.org/citations/22450169 | http://purl.uniprot.org/core/author | "Sudnitsyna M.V."xsd:string |
| http://purl.uniprot.org/citations/22450169 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22450169 | http://purl.uniprot.org/core/name | "Arch Biochem Biophys"xsd:string |
| http://purl.uniprot.org/citations/22450169 | http://purl.uniprot.org/core/pages | "62-70"xsd:string |
| http://purl.uniprot.org/citations/22450169 | http://purl.uniprot.org/core/title | "Cofilin weakly interacts with 14-3-3 and therefore can only indirectly participate in regulation of cell motility by small heat shock protein HspB6 (Hsp20)."xsd:string |
| http://purl.uniprot.org/citations/22450169 | http://purl.uniprot.org/core/volume | "521"xsd:string |
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