| http://purl.uniprot.org/citations/28320860 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/28320860 | http://www.w3.org/2000/01/rdf-schema#comment | "Microtubules are polar cytoskeleton filaments that extend via growth at their plus ends. Microtubule plus-end-tracking proteins (+TIPs) accumulate at these growing plus ends to control microtubule dynamics and attachment. The +TIP end-binding protein 1 (EB1) and its homologs possess an autonomous plus-end-tracking mechanism and interact with other known +TIPs, which then recruit those +TIPs to the growing plus ends. A major +TIP class contains the SXIP (Ser-X-Ile-Pro, with X denoting any amino acid residue) motif, known to interact with EB1 and its homologs for plus-end tracking, but the role of SXIP in regulating EB1 activities is unclear. We show here that an interaction of EB1 with the SXIP-containing +TIP CDK5 regulatory subunit-associated protein 2 (CDK5RAP2) regulates several EB1 activities, including microtubule plus-end tracking, dynamics at microtubule plus ends, microtubule and α/β-tubulin binding, and microtubule polymerization. The SXIP motif fused with a dimerization domain from CDK5RAP2 significantly enhanced EB1 plus-end-tracking and microtubule-polymerizing and bundling activities, but the SXIP motif alone failed to do so. An SXIP-binding-deficient EB1 mutant displayed significantly lower microtubule plus-end tracking than the wild-type protein in transfected cells. These results suggest that EB1 cooperates with CDK5RAP2 and perhaps other SXIP-containing +TIPs in tracking growing microtubule tips. We also generated plus-end-tracking chimeras of CDK5RAP2 and the adenomatous polyposis coli protein (APC) and found that overexpression of the dimerization domains interfered with microtubule plus-end tracking of their respective SXIP-containing chimeras. Our results suggest that disruption of SXIP dimerization enables detailed investigations of microtubule plus-end-associated functions of individual SXIP-containing +TIPs."xsd:string |
| http://purl.uniprot.org/citations/28320860 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m116.759746"xsd:string |
| http://purl.uniprot.org/citations/28320860 | http://purl.uniprot.org/core/author | "Jia Y."xsd:string |
| http://purl.uniprot.org/citations/28320860 | http://purl.uniprot.org/core/author | "Zhou L."xsd:string |
| http://purl.uniprot.org/citations/28320860 | http://purl.uniprot.org/core/author | "Yang S."xsd:string |
| http://purl.uniprot.org/citations/28320860 | http://purl.uniprot.org/core/author | "Qi R.Z."xsd:string |
| http://purl.uniprot.org/citations/28320860 | http://purl.uniprot.org/core/author | "Fong K.W."xsd:string |
| http://purl.uniprot.org/citations/28320860 | http://purl.uniprot.org/core/author | "Au F.K.C."xsd:string |
| http://purl.uniprot.org/citations/28320860 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
| http://purl.uniprot.org/citations/28320860 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/28320860 | http://purl.uniprot.org/core/pages | "7675-7687"xsd:string |
| http://purl.uniprot.org/citations/28320860 | http://purl.uniprot.org/core/title | "Microtubule plus-end tracking of end-binding protein 1 (EB1) is regulated by CDK5 regulatory subunit-associated protein 2."xsd:string |
| http://purl.uniprot.org/citations/28320860 | http://purl.uniprot.org/core/volume | "292"xsd:string |
| http://purl.uniprot.org/citations/28320860 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/28320860 |
| http://purl.uniprot.org/citations/28320860 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/28320860 |
| http://purl.uniprot.org/uniprot/#_A0A0A0MRG9-mappedCitation-28320860 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28320860 |
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