5M50
Mechanism of microtubule minus-end recognition and protection by CAMSAP proteins
Summary for 5M50
| Entry DOI | 10.2210/pdb5m50/pdb |
| EMDB information | 4154 |
| Descriptor | Tubulin alpha chain, Tubulin beta-2B chain, Calmodulin-regulated spectrin-associated protein 3, ... (8 entities in total) |
| Functional Keywords | camsap ckk microtubule tubulin, structural protein |
| Biological source | Mus musculus (Mouse) More |
| Cellular location | Cytoplasm, cytoskeleton : F2Z4C1 Q6B856 Cell junction, adherens junction : Q80VC9 |
| Total number of polymer chains | 5 |
| Total formula weight | 210542.44 |
| Authors | Akhmanova, A.,Moores, C.A.,Baldus, M.,Steinmetz, M.O.,Topf, M.,Roberts, A.J.,Grant, B.J.,Scarabelli, G.,Joseph, A.-P.,van Hooff, J.J.E.,Houben, K.,Hua, S.,Luo, Y.,Stangier, M.M.,Jiang, K.,Atherton, J. (deposition date: 2016-10-20, release date: 2017-10-04, Last modification date: 2024-05-15) |
| Primary citation | Atherton, J.,Jiang, K.,Stangier, M.M.,Luo, Y.,Hua, S.,Houben, K.,van Hooff, J.J.E.,Joseph, A.P.,Scarabelli, G.,Grant, B.J.,Roberts, A.J.,Topf, M.,Steinmetz, M.O.,Baldus, M.,Moores, C.A.,Akhmanova, A. A structural model for microtubule minus-end recognition and protection by CAMSAP proteins. Nat. Struct. Mol. Biol., 24:931-943, 2017 Cited by PubMed Abstract: CAMSAP and Patronin family members regulate microtubule minus-end stability and localization and thus organize noncentrosomal microtubule networks, which are essential for cell division, polarization and differentiation. Here, we found that the CAMSAP C-terminal CKK domain is widely present among eukaryotes and autonomously recognizes microtubule minus ends. Through a combination of structural approaches, we uncovered how mammalian CKK binds between two tubulin dimers at the interprotofilament interface on the outer microtubule surface. In vitro reconstitution assays combined with high-resolution fluorescence microscopy and cryo-electron tomography suggested that CKK preferentially associates with the transition zone between curved protofilaments and the regular microtubule lattice. We propose that minus-end-specific features of the interprotofilament interface at this site serve as the basis for CKK's minus-end preference. The steric clash between microtubule-bound CKK and kinesin motors explains how CKK protects microtubule minus ends against kinesin-13-induced depolymerization and thus controls the stability of free microtubule minus ends. PubMed: 28991265DOI: 10.1038/nsmb.3483 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (5.3 Å) |
Structure validation
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