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KIF11 UFMylation Maintains Photoreceptor Cilium Integrity and Retinal Homeostasis.
- Source :
-
Advanced Science . 7/3/2024, Vol. 11 Issue 25, p1-15. 15p. - Publication Year :
- 2024
-
Abstract
- The photoreceptor cilium is vital for maintaining the structure and function of the retina. However, the molecular mechanisms underlying the photoreceptor cilium integrity and retinal homeostasis are largely unknown. Herein, it is shown that kinesin family member 11 (KIF11) localizes at the transition zone (connecting cilium) of the photoreceptor and plays a crucial role in orchestrating the cilium integrity. KIF11 depletion causes malformations of both the photoreceptor ciliary axoneme and membranous discs, resulting in photoreceptor degeneration and the accumulation of drusen‐like deposits throughout the retina. Mechanistic studies show that the stability of KIF11 is regulated by an interplay between its UFMylation and ubiquitination; UFMylation of KIF11 at lysine 953 inhibits its ubiquitination by synoviolin 1 and thereby prevents its proteasomal degradation. The lysine 953‐to‐arginine mutant of KIF11 is more stable than wild‐type KIF11 and also more effective in reversing the ciliary and retinal defects induced by KIF11 depletion. These findings identify a critical role for KIF11 UFMylation in the maintenance of photoreceptor cilium integrity and retinal homeostasis. [ABSTRACT FROM AUTHOR]
- Subjects :
- *CILIA & ciliary motion
*PHOTORECEPTORS
*HOMEOSTASIS
*UBIQUITINATION
*KINESIN
Subjects
Details
- Language :
- English
- ISSN :
- 21983844
- Volume :
- 11
- Issue :
- 25
- Database :
- Academic Search Index
- Journal :
- Advanced Science
- Publication Type :
- Academic Journal
- Accession number :
- 178228942
- Full Text :
- https://doi.org/10.1002/advs.202400569