http://purl.uniprot.org/citations/10601340 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/10601340 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/10601340 | http://www.w3.org/2000/01/rdf-schema#comment | "We cloned and characterized a full-length cDNA of mouse actin cross-linking family 7 (mACF7) by sequential rapid amplification of cDNA ends-PCR. The completed mACF7 cDNA is 17 kb and codes for a 608-kD protein. The closest relative of mACF7 is the Drosophila protein Kakapo, which shares similar architecture with mACF7. mACF7 contains a putative actin-binding domain and a plakin-like domain that are highly homologous to dystonin (BPAG1-n) at its NH(2) terminus. However, unlike dystonin, mACF7 does not contain a coiled-coil rod domain; instead, the rod domain of mACF7 is made up of 23 dystrophin-like spectrin repeats. At its COOH terminus, mACF7 contains two putative EF-hand calcium-binding motifs and a segment homologous to the growth arrest-specific protein, Gas2. In this paper, we demonstrate that the NH(2)-terminal actin-binding domain of mACF7 is functional both in vivo and in vitro. More importantly, we found that the COOH-terminal domain of mACF7 interacts with and stabilizes microtubules. In transfected cells full-length mACF7 can associate not only with actin but also with microtubules. Hence, we suggest a modified name: MACF (microtubule actin cross-linking factor). The properties of MACF are consistent with the observation that mutations in kakapo cause disorganization of microtubules in epidermal muscle attachment cells and some sensory neurons."xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.org/dc/terms/identifier | "doi:10.1083/jcb.147.6.1275"xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.org/dc/terms/identifier | "doi:10.1083/jcb.147.6.1275"xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/author | "Sun D."xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/author | "Sun D."xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/author | "Zheng M."xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/author | "Zheng M."xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/author | "Liem R.K.H."xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/author | "Liem R.K.H."xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/author | "Leung C.L."xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/author | "Leung C.L."xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/author | "Knowles D.R."xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/author | "Knowles D.R."xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/name | "J. Cell Biol."xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/name | "J. Cell Biol."xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/pages | "1275-1286"xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/pages | "1275-1286"xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/title | "Microtubule actin cross-linking factor (MACF): a hybrid of dystonin and dystrophin that can interact with the actin and microtubule cytoskeletons."xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/title | "Microtubule actin cross-linking factor (MACF): a hybrid of dystonin and dystrophin that can interact with the actin and microtubule cytoskeletons."xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/volume | "147"xsd:string |
http://purl.uniprot.org/citations/10601340 | http://purl.uniprot.org/core/volume | "147"xsd:string |