Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230, Odense M, Denmark.
Membrane Integrity, Danish Cancer Society Research Center, Strandboulevarden 49, 2100, Copenhagen, Denmark.
Sci Rep. 2022 Dec 29;12(1):22568. doi: 10.1038/s41598-022-26633-w.
Efficient plasma membrane repair (PMR) is required to repair damage sustained in the cellular life cycle. The annexin family of proteins, involved in PMR, are activated by Ca influx from extracellular media at the site of injury. Mechanistic studies of the annexins have been overwhelmingly performed using a single annexin, despite the recruitment of multiple annexins to membrane damage sites in living cells. Hence, we investigate the effect of the presence of the crosslinking annexins, annexin A1, A2 and A6 (ANXA1, ANXA2 and ANXA6) on the membrane curvature induction of annexin A4 (ANXA4) in model membrane systems. Our data support a mechanistic model of PMR where ANXA4 induced membrane curvature and ANXA6 crosslinking promotes wound closure. The model now can be expanded to include ANXA1 and ANXA2 as specialist free edge membrane crosslinkers that act in concert with ANXA4 induced curvature and ANXA6 crosslinking.
有效的质膜修复（PMR）对于修复细胞生命周期中受到的损伤是必需的。参与 PMR 的膜联蛋白家族蛋白通过损伤部位细胞外介质中的 Ca 内流而被激活。尽管在活细胞中，多个膜联蛋白被募集到膜损伤部位，但对膜联蛋白的研究绝大多数都是使用单个膜联蛋白进行的。因此，我们研究了交联膜联蛋白，即膜联蛋白 A1、A2 和 A6（ANXA1、ANXA2 和 ANXA6）的存在对模型膜系统中膜联蛋白 A4（ANXA4）诱导的膜曲率的影响。我们的数据支持 PMR 的一种机制模型，其中 ANXA4 诱导膜曲率，而 ANXA6 交联促进伤口闭合。现在可以将该模型扩展到包括 ANXA1 和 ANXA2，它们作为专业的游离边缘膜交联剂，与 ANXA4 诱导的曲率和 ANXA6 交联协同作用。
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