期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 24, 期 11, 页码 931-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3483
关键词
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资金
- ERC [609822]
- Medical Research Council, UK [MR/J000973/1, MR/M019292/1]
- Wellcome Trust
- Royal Society [104196/Z/14/Z]
- National Institutes of Health [R01GM070862]
- Netherlands Organization for Scientific Research (NWO) [718.015.001, 184.032.207]
- uNMR-NL, an NWO [184.032.207]
- Swiss National Science Foundation [31003A_166608]
- SystemsX.ch (RTD-TubeX)
- Biotechnology and Biological Sciences Research Council [BB/K01692X/1] Funding Source: researchfish
- Medical Research Council [MR/J000973/1, MR/M019292/1, MR/R000352/1, G0600084] Funding Source: researchfish
- BBSRC [BB/K01692X/1] Funding Source: UKRI
- MRC [MR/J000973/1, MR/M019292/1, G0600084] Funding Source: UKRI
- European Research Council (ERC) [609822] Funding Source: European Research Council (ERC)
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.
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