| http://purl.uniprot.org/citations/12529434 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12529434 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12529434 | http://www.w3.org/2000/01/rdf-schema#comment | "Although conserved counterparts for most proteins involved in the G(2)/M transition of the cell cycle have been found in all eukaryotes, a notable exception is the essential but functionally enigmatic fungal kinase NIMA. While a number of vertebrate kinases have been identified with catalytic domain homology to NIMA, none of these resemble NIMA within its extensive noncatalytic region, a region critical for NIMA function in Aspergillus nidulans. We used a bioinformatics approach to search for proteins with homology to the noncatalytic region of NIMA and identified mixed lineage kinase 3 (MLK3). MLK3 has been proposed to serve as a component in MAP kinase cascades, particularly those resulting in the activation of the c-Jun N-terminal kinase (JNK). Here we describe the first in-depth study of endogenous MLK3 and report that, like NIMA, MLK3 phosphorylation and activity are enhanced during G(2)/M, whereas JNK remains inactive. Coincident with the G(2)/M transition, a period marked by dramatic reorganization of the cytoplasmic microtubule network, endogenous MLK3 transiently disperses away from the centrosome and centrosomal-proximal sites where it is localized during interphase. Furthermore, when overexpressed, MLK3, like NIMA, localizes to the centrosomal region, induces profound disruption of cytoplasmic microtubules and a nuclear distortion phenotype that differs from mitotic chromosome condensation. Cellular depletion of MLK3 protein using siRNA technology results in an increased sensitivity to the microtubule-stabilizing agent taxol. Our studies suggest a new role for MLK3, separable from its function in the JNK pathway, that may contribute to promoting microtubule instability, a hallmark of M phase entry."xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://purl.org/dc/terms/identifier | "doi:10.1091/mbc.e02-02-0115"xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://purl.org/dc/terms/identifier | "doi:10.1091/mbc.e02-02-0115"xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://purl.uniprot.org/core/author | "Means A.R."xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://purl.uniprot.org/core/author | "Means A.R."xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://purl.uniprot.org/core/author | "Swenson K.I."xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://purl.uniprot.org/core/author | "Swenson K.I."xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://purl.uniprot.org/core/author | "Winkler K.E."xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://purl.uniprot.org/core/author | "Winkler K.E."xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12529434 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12529434 | http://purl.uniprot.org/core/name | "Mol. Biol. Cell"xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://purl.uniprot.org/core/name | "Mol. Biol. Cell"xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://purl.uniprot.org/core/pages | "156-172"xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://purl.uniprot.org/core/pages | "156-172"xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://purl.uniprot.org/core/title | "A new identity for MLK3 as an NIMA-related, cell cycle-regulated kinase that is localized near centrosomes and influences microtubule organization."xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://purl.uniprot.org/core/title | "A new identity for MLK3 as an NIMA-related, cell cycle-regulated kinase that is localized near centrosomes and influences microtubule organization."xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://purl.uniprot.org/core/volume | "14"xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://purl.uniprot.org/core/volume | "14"xsd:string |
| http://purl.uniprot.org/citations/12529434 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12529434 |
| http://purl.uniprot.org/citations/12529434 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12529434 |
| http://purl.uniprot.org/citations/12529434 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12529434 |
| http://purl.uniprot.org/citations/12529434 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12529434 |