DYF-5/MAK-dependent phosphorylation promotes ciliary tubulin unloading.
| 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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| Items | – Name: Title Label: Title Group: Ti Data: DYF-5/MAK-dependent phosphorylation promotes ciliary tubulin unloading. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Xuguang+Jiang%22">Xuguang Jiang</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Wenxin+Shao%22">Wenxin Shao</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Yongping+Chai%22">Yongping Chai</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Jingying+Huang%22">Jingying Huang</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Mohamed%2C+Mohamed+A%2E+A%2E%22">Mohamed, Mohamed A. A.</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Ökten%2C+Zeynep%22">Ökten, Zeynep</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Wei+Li%22">Wei Li</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Zhiwen+Zhu%22">Zhiwen Zhu</searchLink><relatesTo>1</relatesTo><i> zhiwenzhu@126.com</i><br /><searchLink fieldCode="AR" term="%22Guangshuo+Ou%22">Guangshuo Ou</searchLink><relatesTo>1</relatesTo> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Proceedings+of+the+National+Academy+of+Sciences+of+the+United+States+of+America%22">Proceedings of the National Academy of Sciences of the United States of America</searchLink>. 8/23/2022, Vol. 119 Issue 34, p1-8. 13p. – Name: Subject Label: Subject Terms Group: Su Data: *<searchLink fieldCode="DE" term="%22TUBULINS%22">TUBULINS</searchLink><br />*<searchLink fieldCode="DE" term="%22CELL+motility%22">CELL motility</searchLink><br />*<searchLink fieldCode="DE" term="%22LOADING+%26+unloading%22">LOADING & unloading</searchLink><br />*<searchLink fieldCode="DE" term="%22MOLECULAR+motor+proteins%22">MOLECULAR motor proteins</searchLink><br />*<searchLink fieldCode="DE" term="%22PHOSPHORYLATION%22">PHOSPHORYLATION</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: 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] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Proceedings of the National Academy of Sciences of the United States of America is the property of National Academy of Sciences and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1073/pnas.2207134119 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 13 StartPage: 1 Subjects: – SubjectFull: TUBULINS Type: general – SubjectFull: CELL motility Type: general – SubjectFull: LOADING & unloading Type: general – SubjectFull: MOLECULAR motor proteins Type: general – SubjectFull: PHOSPHORYLATION Type: general Titles: – TitleFull: DYF-5/MAK-dependent phosphorylation promotes ciliary tubulin unloading. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Xuguang Jiang – PersonEntity: Name: NameFull: Wenxin Shao – PersonEntity: Name: NameFull: Yongping Chai – PersonEntity: Name: NameFull: Jingying Huang – PersonEntity: Name: NameFull: Mohamed, Mohamed A. A. – PersonEntity: Name: NameFull: Ökten, Zeynep – PersonEntity: Name: NameFull: Wei Li – PersonEntity: Name: NameFull: Zhiwen Zhu – PersonEntity: Name: NameFull: Guangshuo Ou IsPartOfRelationships: – BibEntity: Dates: – D: 23 M: 08 Text: 8/23/2022 Type: published Y: 2022 Identifiers: – Type: issn-print Value: 00278424 Numbering: – Type: volume Value: 119 – Type: issue Value: 34 Titles: – TitleFull: Proceedings of the National Academy of Sciences of the United States of America Type: main |
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