http://purl.uniprot.org/citations/16923827 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16923827 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16923827 | http://www.w3.org/2000/01/rdf-schema#comment | "The spindle pole body (SPB) is the sole site of microtubule nucleation in Saccharomyces cerevisiae; yet, details of its assembly are poorly understood. Integral membrane proteins including Mps2 anchor the soluble core SPB in the nuclear envelope. Adjacent to the core SPB is a membrane-associated SPB substructure known as the half-bridge, where SPB duplication and microtubule nucleation during G1 occurs. We found that the half-bridge component Mps3 is the budding yeast member of the SUN protein family (Sad1-UNC-84 homology) and provide evidence that it interacts with the Mps2 C terminus to tether the half-bridge to the core SPB. Mutants in the Mps3 SUN domain or Mps2 C terminus have SPB duplication and karyogamy defects that are consistent with the aberrant half-bridge structures we observe cytologically. The interaction between the Mps3 SUN domain and Mps2 C terminus is the first biochemical link known to connect the half-bridge with the core SPB. Association with Mps3 also defines a novel function for Mps2 during SPB duplication."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.org/dc/terms/identifier | "doi:10.1083/jcb.200601062"xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.org/dc/terms/identifier | "doi:10.1083/jcb.200601062"xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/author | "Glazko G."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/author | "Glazko G."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/author | "Mushegian A."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/author | "Mushegian A."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/author | "Winey M."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/author | "Winey M."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/author | "Giddings T.H. Jr."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/author | "Giddings T.H. Jr."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/author | "Jaspersen S.L."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/author | "Jaspersen S.L."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/author | "Morgan G."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/author | "Morgan G."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/author | "Martin A.E."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/author | "Martin A.E."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/name | "J. Cell Biol."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/name | "J. Cell Biol."xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/pages | "665-675"xsd:string |
http://purl.uniprot.org/citations/16923827 | http://purl.uniprot.org/core/pages | "665-675"xsd:string |