Focal adhesions contain three specialized actin nanoscale layers

Bibliographic Details
Title: Focal adhesions contain three specialized actin nanoscale layers
Authors: Reena Kumari, Katharina Ven, Megan Chastney, Shrikant B. Kokate, Johan Peränen, Jesse Aaron, Konstantin Kogan, Leonardo Almeida-Souza, Elena Kremneva, Renaud Poincloux, Teng-Leong Chew, Peter W. Gunning, Johanna Ivaska, Pekka Lappalainen
Source: Nature Communications, Vol 15, Iss 1, Pp 1-20 (2024)
Publisher Information: Nature Portfolio, 2024.
Publication Year: 2024
Collection: LCC:Science
Subject Terms: Science
More Details: Abstract Focal adhesions (FAs) connect inner workings of cell to the extracellular matrix to control cell adhesion, migration and mechanosensing. Previous studies demonstrated that FAs contain three vertical layers, which connect extracellular matrix to the cytoskeleton. By using super-resolution iPALM microscopy, we identify two additional nanoscale layers within FAs, specified by actin filaments bound to tropomyosin isoforms Tpm1.6 and Tpm3.2. The Tpm1.6-actin filaments, beneath the previously identified α-actinin cross-linked actin filaments, appear critical for adhesion maturation and controlled cell motility, whereas the adjacent Tpm3.2-actin filament layer beneath seems to facilitate adhesion disassembly. Mechanistically, Tpm3.2 stabilizes ACF-7/MACF1 and KANK-family proteins at adhesions, and hence targets microtubule plus-ends to FAs to catalyse their disassembly. Tpm3.2 depletion leads to disorganized microtubule network, abnormally stable FAs, and defects in tail retraction during migration. Thus, FAs are composed of distinct actin filament layers, and each may have specific roles in coupling adhesions to the cytoskeleton, or in controlling adhesion dynamics.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 2041-1723
Relation: https://doaj.org/toc/2041-1723
DOI: 10.1038/s41467-024-46868-7
Access URL: https://doaj.org/article/52ca205f2286428288ed7a744d2eb902
Accession Number: edsdoj.52ca205f2286428288ed7a744d2eb902
Database: Directory of Open Access Journals
More Details
ISSN:20411723
DOI:10.1038/s41467-024-46868-7
Published in:Nature Communications
Language:English