8C5C
microtubule decorated with tubulin oligomers in presence of APC C-terminal domain. (here only map corresponding to the 13-pf microtubule is represented)
This is a non-PDB format compatible entry.
Summary for 8C5C
Entry DOI | 10.2210/pdb8c5c/pdb |
EMDB information | 16435 16436 |
Descriptor | Tubulin beta chain, Tubulin alpha-1B chain, TAXOL, ... (6 entities in total) |
Functional Keywords | cytoskeleton, microtubule, cell cycle |
Biological source | Bos taurus (cattle) More |
Total number of polymer chains | 52 |
Total formula weight | 2629813.24 |
Authors | |
Primary citation | Serre, L.,Delaroche, J.,Vinit, A.,Schoehn, G.,Denarier, E.,Fourest-Lieuvin, A.,Arnal, I. The mitotic role of adenomatous polyposis coli requires its bilateral interaction with tubulin and microtubules. J.Cell.Sci., 136:-, 2023 Cited by PubMed Abstract: Adenomatous polyposis coli (APC) is a scaffold protein with tumour suppressor properties. Mutations causing the loss of its C-terminal domain (APC-C), which bears cytoskeleton-regulating sequences, correlate with colorectal cancer. The cellular roles of APC in mitosis are widely studied, but the molecular mechanisms of its interaction with the cytoskeleton are poorly understood. Here, we investigated how APC-C regulates microtubule properties, and found that it promotes both microtubule growth and shrinkage. Strikingly, APC-C accumulates at shrinking microtubule extremities, a common characteristic of depolymerases. Cryo-electron microscopy revealed that APC-C adopts an extended conformation along the protofilament crest and showed the presence of ring-like tubulin oligomers around the microtubule wall, which required the presence of two APC-C sub-domains. A mutant of APC-C that was incapable of decorating microtubules with ring-like tubulin oligomers exhibited a reduced effect on microtubule dynamics. Finally, whereas native APC-C rescued defective chromosome alignment in metaphase cells silenced for APC, the ring-incompetent mutant failed to correct mitotic defects. Thus, the bilateral interaction of APC-C with tubulin and microtubules likely contributes to its mitotic functions. PubMed: 36541084DOI: 10.1242/jcs.260152 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (5.3 Å) |
Structure validation
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