Abstract：
Contractile actomyosin bundles play crucial roles in various physiological processes, including cell migration, morphogenesis, and muscle contraction. The intricate assembly of actomyosin bundles involves the precise alignment and fusion of myosin II filaments, yet the underlying mechanisms and factors involved in these processes remain elusive. Our study reveals that LUZP1 plays a central role in orchestrating the maturation of thick actomyosin bundles. Loss of LUZP1 caused abnormal cell morphogenesis, migration, and the ability to exert forces on the environment. Importantly, knockout of LUZP1 results in significant defects in the concatenation and persistent association of myosin II filaments, severely impairing the assembly of myosin II stacks. The disruption of these processes in LUZP1 knockout cells provides mechanistic insights into the defective assembly of thick ventral stress fibers and the associated cellular contractility abnormalities. Overall, these results significantly contribute to our understanding of the molecular mechanism involved in actomyosin bundle formation and highlight the essential role of LUZP1 in this process.
摘要：
收缩肌球蛋白束在各种生理过程中起着至关重要的作用，包括细胞迁移，形态发生,肌肉收缩。肌动球蛋白束的复杂组装涉及肌球蛋白II丝的精确排列和融合，然而，这些过程中涉及的潜在机制和因素仍然难以捉摸。我们的研究表明，LUZP1在协调厚实肌球蛋白束的成熟中起着核心作用。LUZP1缺失导致细胞形态发生异常，迁移,以及对环境施加力量的能力。重要的是,敲除LUZP1导致肌球蛋白II细丝的串联和持续关联的显着缺陷，严重损害肌球蛋白II堆栈的组装。LUZP1敲除细胞中这些过程的破坏提供了对厚的腹侧应力纤维的缺陷组装和相关的细胞收缩异常的机械见解。总的来说,这些结果极大地有助于我们对肌动球蛋白束形成的分子机制的理解，并强调了LUZP1在这一过程中的重要作用。
