AI Article Synopsis
- GTPases switch between active (GTP-bound) and inactive (GDP-bound) states, with GEFs facilitating GDP-GTP exchange and GAPs speeding up GTP hydrolysis.
- The RacGEF PIX-1 is essential for forming integrin adhesion complexes in muscle cells, and its proper function is linked to structures like muscle cell boundaries and dense bodies.
- Mutations in RhoGAP proteins disrupt IAC assembly and result in muscle disorganization and reduced movement, highlighting RRC-1's role as a crucial RhoGAP in conjunction with PIX-1.
Article Abstract
GTPases cycle between active GTP bound and inactive GDP bound forms. Exchange of GDP for GTP is catalyzed by guanine nucleotide exchange factors (GEFs). GTPase activating proteins (GAPs) accelerate GTP hydrolysis, to promote the GDP bound form. We reported that the RacGEF, PIX-1, is required for assembly of integrin adhesion complexes (IAC) in striated muscle of . In , IACs are found at the muscle cell boundaries (MCBs), and bases of sarcomeric M-lines and dense bodies (Z-disks). Screening mutants in proteins containing RhoGAP domains revealed that loss of function of results in loss of IAC components at MCBs, disorganization of M-lines and dense bodies, and reduced whole animal locomotion. RRC-1 localizes to MCBs, like PIX-1. The localization of RRC-1 at MCBs requires PIX-1, and the localization of PIX-1 requires RRC-1. Loss of function of CED-10 (Rac) shows lack of PIX-1 and RRC-1 at MCBs. RRC-1 exists in a complex with PIX-1. Transgenic rescue of was achieved with wild type RRC-1 but not RRC-1 with a missense mutation in a highly conserved residue of the RhoGAP domain. Our results are consistent with RRC-1 being a RhoGAP for the PIX pathway in muscle.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11064667 | PMC |
| http://dx.doi.org/10.1091/mbc.E23-03-0095 | DOI Listing |
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