| Title: |
DYF-5/MAK-dependent phosphorylation promotes ciliary tubulin unloading. |
| Authors: |
Xuguang Jiang1, Wenxin Shao1, Yongping Chai1, Jingying Huang1, Mohamed, Mohamed A. A.2, Ökten, Zeynep2, Wei Li3, Zhiwen Zhu1 zhiwenzhu@126.com, Guangshuo Ou1 |
| Source: |
Proceedings of the National Academy of Sciences of the United States of America. 8/23/2022, Vol. 119 Issue 34, p1-8. 13p. |
| Subject Terms: |
*TUBULINS, *CELL motility, *LOADING & unloading, *MOLECULAR motor proteins, *PHOSPHORYLATION |
| Abstract: |
Cilia are microtubule-based organelles that power cell motility and regulate sensation and signaling, and abnormal ciliary structure and function cause various ciliopathies. Cilium formation and maintenance requires intraflagellar transport (IFT), during which the kinesin-2 family motor proteins ferry IFT particles carrying axonemal precursors such as tubulins into cilia. Tubulin dimers are loaded to IFT machinery through an interaction between tubulin and the IFT-74/81 module; however, little is known of how tubulins are unloaded when arriving at the ciliary tip. Here, we show that the ciliary kinase DYF-5/MAK phosphorylates multiple sites within the tubulin-binding module of IFT-74, reducing the tubulin-binding affinity of IFT-74/81 approximately sixfold. Ablation or constitutive activation of IFT-74 phosphorylation abnormally elongates or shortens sensory cilia in Caenorhabditis elegans neurons. We propose that DYF-5/MAK-dependent phosphorylation plays a fundamental role in ciliogenesis by regulating tubulin unloading. [ABSTRACT FROM AUTHOR] |
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| Database: |
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