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http://purl.uniprot.org/citations/17166838http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17166838http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17166838http://www.w3.org/2000/01/rdf-schema#comment"HAP1 (Huntingtin-associated protein 1) consists of two alternately spliced isoforms (HAP1A and HAP1B, which have unique C-terminal sequences) and participates in intracellular trafficking. The C terminus of HAP1A is phosphorylated, and this phosphorylation was found to decrease the association of HAP1A with kinesin light chain, a protein involved in anterograde transport in cells. It remains unclear how this phosphorylation functions to regulate the association of HAP1 with trafficking proteins. Using the yeast two-hybrid system, we found that HAP1 also interacts with 14-3-3 proteins, which are involved in the assembly of protein complexes and the regulation of protein trafficking. The interaction of HAP1 with 14-3-3 is confirmed by their immunoprecipitation and colocalization in mouse brain. Moreover, this interaction is specific to HAP1A and is increased by the phosphorylation of the C terminus of HAP1A. We also found that expression of 14-3-3 decreases the association of HAP1A with kinesin light chain. As a result, there is less HAP1A distributed in neurite tips of PC12 cells that overexpress 14-3-3. Also, overexpression of 14-3-3 reduces the effect of HAP1A in promoting neurite outgrowth of PC12 cells. We propose that the phosphorylation-dependent interaction of HAP1A with 14-3-3 regulates HAP1 function by influencing its association with kinesin light chain and trafficking in neuronal processes."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m609057200"xsd:string
http://purl.uniprot.org/citations/17166838http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m609057200"xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/author"Fu H."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/author"Fu H."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/author"Li S."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/author"Li S."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/author"Li M."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/author"Li M."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/author"Sheng G."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/author"Sheng G."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/author"Wu M."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/author"Wu M."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/author"Li X.J."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/author"Li X.J."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/author"Rong J."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/author"Rong J."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/author"Coblitz B."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/author"Coblitz B."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17166838http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string