2025-06-15 清華大学
Figure 1. Diagram of proposed model on how phosphorylation regulates regional motility of ciliary kinesin OSM-3 (t.z.: transition zone; m.s.: middle segment; d.s.: distal segment).
<関連情報>
- https://www.tsinghua.edu.cn/en/info/1245/14309.htm
- https://rupress.org/jcb/article-abstract/224/7/e202407152/277655/Phosphorylation-dependent-regional-motility-of-the
リン酸化に依存した毛様体キネシンOSM-3の領域運動性
Phosphorylation-dependent regional motility of the ciliary kinesin OSM-3
Peng Huang,Guanghan Chen,Zhiwen Zhu,Shimin Wang,Zhe Chen,Yongping Chai,Wei Li,Guangshuo Ou
Journal of Cell Biology Published:April 24 2025
DOI:https://doi.org/10.1083/jcb.202407152
Kinesin motor proteins, vital for intracellular microtubule-based transport, display region-specific motility within cells, a phenomenon that remains molecularly enigmatic. This study focuses on the localized activation of OSM-3, an intraflagellar transport kinesin crucial for the assembly of ciliary distal segments in Caenorhabditis elegans sensory neurons. Fluorescence lifetime imaging microscopy unveiled an extended, active conformation of OSM-3 in the ciliary base and middle segments, where OSM-3 is conveyed as cargo by kinesin-II. We demonstrate that NEKL-3, a never in mitosis kinase-like protein, directly phosphorylates the motor domain of OSM-3, inhibiting its in vitro activity. NEKL-3 and NEKL-4, localized at the ciliary base, function redundantly to restrict OSM-3 activation. Elevated levels of protein phosphatase 2A at the ciliary transition zone or middle segments triggered premature OSM-3 motility, while its deficiency resulted in reduced OSM-3 activity and shorter cilia. These findings elucidate a phosphorylation-mediated mechanism governing the regional motility of kinesins.
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