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6IW8

Crystal structure of Importin-alpha and wild-type GM130

Summary for 6IW8
Entry DOI10.2210/pdb6iw8/pdb
DescriptorPeptide from Golgin subfamily A member 2, Importin subunit alpha-1 (3 entities in total)
Functional Keywordsimportin alpha, gm130, protein binding
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains2
Total formula weight52668.27
Authors
Chang, C.-C.,Chen, C.-J.,Pien, Y.-C.,Tsai, S.-Y.,Hsia, K.-C. (deposition date: 2018-12-04, release date: 2019-10-02, Last modification date: 2023-11-22)
Primary citationChang, C.-C.,Chen, C.-J.,Grauffel, C.,Pien, Y.-C.,Lim, C.,Tsai, S.-Y.,Hsia, K.-C.
Ran pathway-independent regulation of mitotic Golgi disassembly by Importin-alpha.
Nat Commun, 10:4307-4307, 2019
Cited by
PubMed Abstract: To facilitate proper mitotic cell partitioning, the Golgi disassembles by suppressing vesicle fusion. However, the underlying mechanism has not been characterized previously. Here, we report a Ran pathway-independent attenuation mechanism that allows Importin-α (a nuclear transport factor) to suppress the vesicle fusion mediated by p115 (a vesicular tethering factor) and is required for mitotic Golgi disassembly. We demonstrate that Importin-α directly competes with p115 for interaction with the Golgi protein GM130. This interaction, promoted by a phosphate moiety on GM130, is independent of Importin-β and Ran. A GM130 K34A mutant, in which the Importin-α-GM130 interaction is specifically disrupted, exhibited abundant Golgi puncta during metaphase. Importantly, a mutant showing enhanced p115-GM130 interaction presented proliferative defects and G2/M arrest, demonstrating that Importin-α-GM130 binding modulates the Golgi disassembly that governs mitotic progression. Our findings illuminate that the Ran and kinase-phosphatase pathways regulate multiple aspects of mitosis coordinated by Importin-α (e.g. spindle assembly, Golgi disassembly).
PubMed: 31541088
DOI: 10.1038/s41467-019-12207-4
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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数据于2024-10-30公开中

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