Cross-regulations of two connected domains form a mechanical circuit for steady force transmission during clathrin-mediated endocytosis.

Autor:	Ren Y; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA; Nanobiology Institute, Yale University, West Haven, CT 06516, USA. Electronic address: yuan.ren@yale.edu., Yang J; Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USA., Fujita B; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA; Nanobiology Institute, Yale University, West Haven, CT 06516, USA., Zhang Y; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA; Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USA. Electronic address: yongli.zhang@yale.edu., Berro J; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA; Nanobiology Institute, Yale University, West Haven, CT 06516, USA; Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USA. Electronic address: julien.berro@yale.edu.
Jazyk:	angličtina
Zdroj:	Cell reports [Cell Rep] 2024 Sep 24; Vol. 43 (9), pp. 114725. Date of Electronic Publication: 2024 Sep 13.
DOI:	10.1016/j.celrep.2024.114725
Abstrakt:	Mechanical forces are transmitted from the actin cytoskeleton to the membrane during clathrin-mediated endocytosis (CME) in the fission yeast Schizosaccharomyces pombe. End4p directly transmits force in CME by binding to both the membrane (through the AP180 N-terminal homology [ANTH] domain) and F-actin (through the talin-HIP1/R/Sla2p actin-tethering C-terminal homology [THATCH] domain). We show that 7 pN force is required for stable binding between THATCH and F-actin. We also characterized a domain in End4p, Rend (rod domain in End4p), that resembles R12 of talin. Membrane localization of Rend primes the binding of THATCH to F-actin, and force-induced unfolding of Rend at 15 pN terminates the transmission of force. We show that the mechanical properties (mechanical stability, unfolding extension, hysteresis) of Rend and THATCH are tuned to form a circuit for the initiation, transmission, and termination of force between the actin cytoskeleton and membrane. The mechanical circuit by Rend and THATCH may be conserved and coopted evolutionarily in cell adhesion complexes. Competing Interests: Declaration of interests J.B., Y.R., and Y.Z. filed a patent application relating to the force sensor presented in this paper (PCT application no. PCT/US23/69505 submitted June 30, 2023, by Yale University [inventors: J.B., Y.R., and Y.Z.]). (Copyright © 2024 The Author(s). Published by Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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