ARAP1 fine-tunes F-actin polymerization level in lymphocytes through RhoA inhibition
Yoshihiro Ueda, Naoyuki Kondo, Yuji Kamioka, Tatsuo Kinashi · 2025
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Description
Yoshihiro Ueda and three co-authors pin down, in a 2025 study, how a protein fine-tunes the inner scaffold of white blood cells. These lymphocytes must crawl toward chemical signals and grip surfaces, which needs fast reshaping of their actin mesh. A switch called RhoA drives much of that reshaping, but its cooperation with related switches was unclear.
The protein, ARAP1, is recruited to cell protrusions after a chemokine signal lands. Cells that lack it migrate faster, with RhoA more active and the actin mesh built up more strongly. Extra ARAP1 has the opposite effect, and it needs the part of the protein that switches RhoA off. A second part of ARAP1 binds two related switches, Rac and Rap1, and is required for the brake on RhoA to work. The authors read ARAP1 as a fine-tuner that sits where the related switches gather.
Catalog record
| CREATOR | Yoshihiro Ueda, Naoyuki Kondo, Yuji Kamioka, Tatsuo Kinashi |
|---|---|
| YEAR | 2025 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 45 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |