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LUZP1 regulates the maturation of contractile actomyosin bundles.
Wang, Liang; Tsang, Hoi Ying; Yan, Ziyi; Tojkander, Sari; Ciuba, Katarzyna; Kogan, Konstantin; Liu, Xiaonan; Zhao, Hongxia.
Affiliation
  • Wang L; Faculty of Biological and Environmental Sciences, University of Helsinki, FI-00014, Helsinki, Finland.
  • Tsang HY; Mental Health Center and National Chengdu Center for Safety Evaluation of Drugs, State Key Laboratory of Biotherapy/Collaborative Innovation Center for Biotherapy, West China Hospital, Sichuan University, Chengdu, 610041, China.
  • Yan Z; Faculty of Biological and Environmental Sciences, University of Helsinki, FI-00014, Helsinki, Finland.
  • Tojkander S; Faculty of Biological and Environmental Sciences, University of Helsinki, FI-00014, Helsinki, Finland.
  • Ciuba K; Department of Veterinary Biosciences, Faculty of Veterinary Medicine, University of Helsinki, Helsinki, Finland.
  • Kogan K; Institute of Biotechnology, University of Helsinki, FI-00014, Helsinki, Finland.
  • Liu X; Institute of Biotechnology, University of Helsinki, FI-00014, Helsinki, Finland.
  • Zhao H; Institute of Biotechnology, University of Helsinki, FI-00014, Helsinki, Finland.
Cell Mol Life Sci ; 81(1): 248, 2024 Jun 04.
Article in En | MEDLINE | ID: mdl-38832964
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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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Actomyosin / Cell Movement / Myosin Type II / Muscle Contraction Limits: Humans Language: En Journal: Cell Mol Life Sci Journal subject: BIOLOGIA MOLECULAR Year: 2024 Document type: Article Affiliation country:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Actomyosin / Cell Movement / Myosin Type II / Muscle Contraction Limits: Humans Language: En Journal: Cell Mol Life Sci Journal subject: BIOLOGIA MOLECULAR Year: 2024 Document type: Article Affiliation country:
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