| http://purl.uniprot.org/citations/21385839 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21385839 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21385839 | http://www.w3.org/2000/01/rdf-schema#comment | "Kinesin light chain 1 (KLC1) binds to the intracellular cytoplasmic domain of the type-1 membrane-spanning protein calsyntenin-1 (also known as alcadein-α) to mediate transport of a subset of vesicles. Here, we identify serine 460 in KLC1 (KLC1ser460) as a phosphorylation site and show that mutation of KLC1ser460 influences the binding of KLC1 to calsyntenin-1. Mutation of KLC1ser460 to an alanine residue, to preclude phosphorylation, increased the binding of calsyntenin-1, whereas mutation to an aspartate residue, to mimic permanent phosphorylation, reduced the binding. Mutation of KLC1ser460 did not affect the interaction of KLC1 with four other known binding partners: huntingtin-associated protein 1 isoform A (HAP1A), collapsin response mediator protein-2 (CRMP2), c-Jun N-terminal kinase-interacting protein-1 (JIP1) and kinase-D-interacting substrate of 220 kDa (Kidins220). KLC1ser460 is a predicted mitogen-activated protein kinase (MAPK) target site, and we show that extracellular-signal-regulated kinase (ERK) phosphorylates this residue in vitro. We also demonstrate that inhibition of ERK promotes binding of calsyntenin-1 to KLC1. Finally, we show that expression of the KLC1ser460 mutant proteins influences calsyntenin-1 distribution and transport in cultured cells. Thus, phosphorylation of KLC1ser460 represents a mechanism for selectively regulating the binding and trafficking of calsyntenin-1."xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.075168"xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.075168"xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/author | "Miller C.C."xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/author | "Miller C.C."xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/author | "Rodriguez L."xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/author | "Rodriguez L."xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/author | "De Vos K.J."xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/author | "De Vos K.J."xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/author | "Manser C."xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/author | "Manser C."xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/author | "Vagnoni A."xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/author | "Vagnoni A."xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/name | "J. Cell Sci."xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/name | "J. Cell Sci."xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/pages | "1032-1042"xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/pages | "1032-1042"xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/title | "Phosphorylation of kinesin light chain 1 at serine 460 modulates binding and trafficking of calsyntenin-1."xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/title | "Phosphorylation of kinesin light chain 1 at serine 460 modulates binding and trafficking of calsyntenin-1."xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/volume | "124"xsd:string |
| http://purl.uniprot.org/citations/21385839 | http://purl.uniprot.org/core/volume | "124"xsd:string |