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Graphpad prism 8 free download mac5/24/2023 ![]() The three major Rho family GTPases-Rho, Rac, and Cdc42-are recruited to wounds in spatially and temporally distinct patterns to carry out specific functions during the repair process 7, 8, 9, 11. ![]() One of the major features of cell wound repair is the assembly of a Rho family GTPase-dependent actomyosin ring at the wound periphery that attaches the cortical cytoskeleton to the overlying plasma membrane, followed by its dynamic translocation inward to pull the cell cortex breach closed 5, 6, 7, 8, 9, 10. These differing spatiotemporal recruitment patterns and wound repair phenotypes highlight the Rac-independent functions of SCAR and provide an exciting new context in which to investigate these newly uncovered SCAR functions.Ĭells encounter physical stresses daily leading to breaks in their cortex that must be rapidly repaired to maintain cell integrity and function 1, 2, 3, 4. ![]() We also show that while Rac is important for actin recruitment to the actomyosin ring, SCAR serves to organize the actomyosin ring and facilitate its anchoring to the overlying plasma membrane. Interestingly, we find that SCAR is recruited to wounds earlier than Rac and is still recruited to the wound periphery in the presence of a potent Rac inhibitor. Here we show that Rac and SCAR are recruited to cell wounds in the Drosophila repair model and are required for the proper formation and maintenance of the dynamic actomyosin ring formed at the wound periphery. In particular, the WAS protein Scar/WAVE has been shown to exhibit one-to-one correspondence with Rac GTPase. Wiskott-Aldrich Syndrome (WAS) family proteins are downstream effectors of Rho family GTPases that usually function in a one-to-one correspondence to regulate branched actin nucleation. Rho family GTPases regulate both linear and branched actin dynamics by activating downstream effectors to facilitate the assembly and function of complex cellular structures such as lamellipodia and contractile actomyosin rings.
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