Molecular basis for CPAP-tubulin interaction in controlling centriolar and ciliary length
Centrioles and cilia are microtubule-based structures of defined architecture, but what regulates this architecture is not clear. Here the authors discover that centrosomal-P4.1-associated-protein (CPAP) binds the α/β-tubulin dimer and licenses it for tubulin delivery contributing to centriolar/cili...
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Nature Portfolio
2016
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oai:doaj.org-article:9be27009a3e84a74ac5a9cc418b64bae2021-12-02T14:40:11ZMolecular basis for CPAP-tubulin interaction in controlling centriolar and ciliary length10.1038/ncomms118742041-1723https://doaj.org/article/9be27009a3e84a74ac5a9cc418b64bae2016-06-01T00:00:00Zhttps://doi.org/10.1038/ncomms11874https://doaj.org/toc/2041-1723Centrioles and cilia are microtubule-based structures of defined architecture, but what regulates this architecture is not clear. Here the authors discover that centrosomal-P4.1-associated-protein (CPAP) binds the α/β-tubulin dimer and licenses it for tubulin delivery contributing to centriolar/ciliary length and architecture control.Xiangdong ZhengAnand RamaniKomal SoniMarco GottardoShuangping ZhengLi Ming GooiWenjing LiShan FengAruljothi MariappanArpit WasonPer WidlundAndrei PozniakovskyIna PoserHaiteng DengGuangshuo OuMaria RiparbelliCallaini GiulianoAnthony A. HymanMichael SattlerJay GopalakrishnanHaitao LiNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-13 (2016) |
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Science Q Xiangdong Zheng Anand Ramani Komal Soni Marco Gottardo Shuangping Zheng Li Ming Gooi Wenjing Li Shan Feng Aruljothi Mariappan Arpit Wason Per Widlund Andrei Pozniakovsky Ina Poser Haiteng Deng Guangshuo Ou Maria Riparbelli Callaini Giuliano Anthony A. Hyman Michael Sattler Jay Gopalakrishnan Haitao Li Molecular basis for CPAP-tubulin interaction in controlling centriolar and ciliary length |
description |
Centrioles and cilia are microtubule-based structures of defined architecture, but what regulates this architecture is not clear. Here the authors discover that centrosomal-P4.1-associated-protein (CPAP) binds the α/β-tubulin dimer and licenses it for tubulin delivery contributing to centriolar/ciliary length and architecture control. |
format |
article |
author |
Xiangdong Zheng Anand Ramani Komal Soni Marco Gottardo Shuangping Zheng Li Ming Gooi Wenjing Li Shan Feng Aruljothi Mariappan Arpit Wason Per Widlund Andrei Pozniakovsky Ina Poser Haiteng Deng Guangshuo Ou Maria Riparbelli Callaini Giuliano Anthony A. Hyman Michael Sattler Jay Gopalakrishnan Haitao Li |
author_facet |
Xiangdong Zheng Anand Ramani Komal Soni Marco Gottardo Shuangping Zheng Li Ming Gooi Wenjing Li Shan Feng Aruljothi Mariappan Arpit Wason Per Widlund Andrei Pozniakovsky Ina Poser Haiteng Deng Guangshuo Ou Maria Riparbelli Callaini Giuliano Anthony A. Hyman Michael Sattler Jay Gopalakrishnan Haitao Li |
author_sort |
Xiangdong Zheng |
title |
Molecular basis for CPAP-tubulin interaction in controlling centriolar and ciliary length |
title_short |
Molecular basis for CPAP-tubulin interaction in controlling centriolar and ciliary length |
title_full |
Molecular basis for CPAP-tubulin interaction in controlling centriolar and ciliary length |
title_fullStr |
Molecular basis for CPAP-tubulin interaction in controlling centriolar and ciliary length |
title_full_unstemmed |
Molecular basis for CPAP-tubulin interaction in controlling centriolar and ciliary length |
title_sort |
molecular basis for cpap-tubulin interaction in controlling centriolar and ciliary length |
publisher |
Nature Portfolio |
publishDate |
2016 |
url |
https://doaj.org/article/9be27009a3e84a74ac5a9cc418b64bae |
work_keys_str_mv |
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1718390371752345600 |