Phosphorylation of Arl4A/D promotes their binding by the HYPK chaperone for their stable recruitment to the plasma membrane

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 119; no. 30; pp. 1 - 9
• Main Authors: Lin, Ming-Chieh, Yu, Chia-Jung, Lee, Fang-Jen S.
• Format: Journal Article
• Language: English
• Published: Washington National Academy of Sciences 26.07.2022
• Subjects: Biological Sciences; Cell adhesion & migration; Cell migration; Cytoskeleton; Degradation; Fibronectin; Guanosine triphosphatases; Kinases; Membranes; Phosphorylation; Proteasomes; Proteins; Proteomics; Recruitment; Regulatory mechanisms (biology); Stability analysis; Stimulation

The Arl4 small GTPases participate in a variety of cellular events, including cytoskeleton remodeling, vesicle trafficking, cell migration, and neuronal development. Whereas small GTPases are typically regulated by their GTPase cycle, Arl4 proteins have been found to act independent of this canonica...