维持细胞活力依赖于质膜的完整性,损坏时必须修理。可溶性N-乙基马来酰亚胺敏感因子附着蛋白受体（SNARE）介导的膜融合是参与膜修复的重要机制。在C.elegans表皮细胞hyp7中，syntaxin-2（SYX-2）促进了大膜伤口的修复；然而，潜在的分子机制尚不清楚.这里,我们发现SNAP-25蛋白RIC-4和突触蛋白SEC-22是伤口部位SYX-2募集所必需的。它们相互作用形成SNARE复合物以促进体内膜修复和体外融合。此外，我们发现SEC-22位于多个细胞内区室，包括内体和跨高尔基网络，招募到伤口。此外，抑制RAB-5破坏SEC-22的定位并阻止其与SYX-2的相互作用。我们的发现表明，RAB-5促进了RIC-4/SEC-22/SYX-2SNARE复合物的形成，并为细胞修复大膜伤口的分子机制提供了有价值的见解。
Maintaining cellular viability relies on the integrity of the plasma membrane, which must be repaired upon damage. Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE)-mediated membrane fusion is a crucial mechanism involved in membrane repair. In C. elegans epidermal cell hyp 7, syntaxin-2 (SYX-2) facilitates large membrane wound repair; however, the underlying molecular mechanism remains unclear. Here, we found that SNAP-25 protein RIC-4 and synaptobrevin protein SEC-22 are required for SYX-2 recruitment at the wound site. They interact to form a SNARE complex to promote membrane repair in vivo and fusion in vitro. Moreover, we found that SEC-22 localized in multiple intracellular compartments, including endosomes and the trans-Golgi network, which recruited to the wounds. Furthermore, inhibition of RAB-5 disrupted SEC-22 localization and prevented its interaction with SYX-2. Our findings suggest that RAB-5 facilitates the formation of the RIC-4/SEC-22/SYX-2 SNARE complex and provides valuable insights into the molecular mechanism of how cells repair large membrane wounds.
