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LUZP1 regulates the maturation of contractile actomyosin bundles. | LitMetric

LUZP1 regulates the maturation of contractile actomyosin bundles.

Cell Mol Life Sci

Faculty of Biological and Environmental Sciences, University of Helsinki, FI-00014, Helsinki, Finland.

Published: June 2024

AI Article Synopsis

  • Contractile actomyosin bundles are essential for various physiological processes like cell migration and muscle contraction, but the exact mechanisms of their assembly are not fully understood.
  • The study identifies LUZP1 as a key player in the maturation of these bundles, with its absence leading to abnormal cell structure and movement.
  • Knockout experiments demonstrate that LUZP1 loss disrupts the assembly of myosin II filaments, revealing important insights into how actomyosin bundles form and their role in cell contractility.

Article 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11335285PMC
http://dx.doi.org/10.1007/s00018-024-05294-0DOI Listing

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