| http://purl.uniprot.org/citations/10744979 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10744979 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10744979 | http://www.w3.org/2000/01/rdf-schema#comment | "The Jun N-terminal kinase (JNK) is a downstream effector of Rac and Cdc42 GTPases involved in actin reorganization [1-3]. A role of the Drosophila JNK homologue, Basket (DJNK/Bsk), in the regulation of cell shape changes and actin reorganization arises from its function in the process of dorsal closure [4-6]. One potential mechanism for induction of cytoskeletal changes by JNK is via transcriptional activation of the decapentaplegic gene (dpp, a member of the TGFbeta superfamily) [6]. A direct link between JNK signalling and actin organization has not yet been found, however. We have identified a novel DJNK-interacting protein, p150-Spir, that belongs to the Wiscott-Aldrich syndrome protein (WASP) homology domain 2 (WH2) family of proteins involved in actin reorganization [7] [8]. It is a multidomain protein with a cluster of four WH2 domains, a modified FYVE zinc-finger motif [9], and a DEJL motif, a docking site for JNK [10], at its carboxy-terminal end. In mouse fibroblasts, p150-Spir colocalized with F-actin and its overexpression induced clustering of filamentous actin around the nucleus. When coexpressed with p150-Spir in NIH 3T3 cells, JNK translocated to and colocalizes with p150-Spir at discrete spots around the nucleus. Carboxy-terminal sequences of p150-Spir were phosphorylated by JNK both in vitro and in vivo. We conclude that p150-Spir is a downstream target of JNK function and provides a direct link between JNK and actin organization."xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0960-9822(00)00388-2"xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0960-9822(00)00388-2"xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/author | "Bork P."xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/author | "Bork P."xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/author | "Rapp U.R."xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/author | "Rapp U.R."xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/author | "Raabe T."xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/author | "Raabe T."xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/author | "Kerkhoff E."xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/author | "Kerkhoff E."xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/author | "Otto I.M."xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/author | "Otto I.M."xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/author | "Rennefahrt U.E.E."xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/author | "Rennefahrt U.E.E."xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/name | "Curr. Biol."xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/name | "Curr. Biol."xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/pages | "345-348"xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/pages | "345-348"xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/title | "The p150-Spir protein provides a link between c-Jun N-terminal kinase function and actin reorganization."xsd:string |
| http://purl.uniprot.org/citations/10744979 | http://purl.uniprot.org/core/title | "The p150-Spir protein provides a link between c-Jun N-terminal kinase function and actin reorganization."xsd:string |