| http://purl.uniprot.org/citations/22074847 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22074847 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22074847 | http://www.w3.org/2000/01/rdf-schema#comment | "Interaction between the mammalian cell polarity proteins mInsc (mammalian homologue of Inscuteable) and Leu-Gly-Asn repeat-enriched protein (LGN), as well as that between their respective Drosophila homologues Inscuteable and Partner of Inscuteable (Pins), plays crucial roles in mitotic spindle orientation, a process contributing to asymmetric cell division. Here, we report a crystal structure of the LGN-binding domain (LBD) of human mInsc complexed with the N-terminal tetratricopeptide repeat (TPR) motifs of human LGN at 2.6-Å resolution. In the complex, mInsc-LBD adopts an elongated structure with three binding modules--an α-helix, an extended region, and a β-sheet connected with a loop--that runs antiparallel to LGN along the concave surface of the superhelix formed by the TPRs. Structural analysis and structure-based mutagenesis define residues that are critical for mInsc-LGN association, and reveal that the activator of G-protein signaling 3 (AGS3)-binding protein Frmpd1 [4.1/ezrin/radixin/moesin (FERM) and PSD-95/Dlg/ZO-1 (PDZ) domain-containing protein 1] and its relative Frmpd4 interact with LGN via a region homologous to a part of mInsc-LBD, whereas nuclear mitotic apparatus protein (NuMA) and the C terminus of LGN recognize the TPR domain in a manner different from that by mInsc. mInsc binds to LGN with the highest affinity (K(D) ≈ 2.4 nM) and effectively replaces the Frmpd proteins, NuMA, and the LGN C terminus, suggesting the priority of mInsc in binding to LGN. We also demonstrate, using mutant proteins, that mInsc-LGN interaction is vital for stabilization of LGN and for intracellular localization of mInsc."xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1110951108"xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1110951108"xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/author | "Yuzawa S."xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/author | "Yuzawa S."xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/author | "Sumimoto H."xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/author | "Sumimoto H."xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/author | "Kamakura S."xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/author | "Kamakura S."xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/author | "Hayase J."xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/author | "Hayase J."xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/author | "Iwakiri Y."xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/author | "Iwakiri Y."xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/pages | "19210-19215"xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/pages | "19210-19215"xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/title | "Structural basis for interaction between the conserved cell polarity proteins Inscuteable and Leu-Gly-Asn repeat-enriched protein (LGN)."xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/title | "Structural basis for interaction between the conserved cell polarity proteins Inscuteable and Leu-Gly-Asn repeat-enriched protein (LGN)."xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/volume | "108"xsd:string |
| http://purl.uniprot.org/citations/22074847 | http://purl.uniprot.org/core/volume | "108"xsd:string |