Journal article
Dynamics of the Actin Cytoskeleton at Adhesion Complexes
Biology (Basel, Switzerland), Vol.11(1), p.52
01/01/2022
DOI: 10.3390/biology11010052
PMCID: PMC8773209
PMID: 35053050
Abstract
Simple Summary All cells in the human body experience force. To withstand these forces, cells rearrange and reinforce their cytoskeletons. In this review, we describe the structure of the actin cytoskeleton and its anchorage at points where cells adhere to the extracellular matrix and one another. We examine the current understanding for how the actin cytoskeleton is remodeled by force. This examination reveals that the response of cells to force is complex and highly coordinated. The shape of cells is altered to allow cells to adapt to their changing environments, including responding to internally generated and externally applied force. Force is sensed by cell surface adhesion proteins that are enriched in sites where cells bind to the extracellular matrix (focal adhesions) and neighboring cells (cell-cell or adherens junctions). Receptors at these adhesion sites stimulate intracellular signal transduction cascades that culminate in dramatic changes in the actin cytoskeleton. New actin filaments form, and/or new and existing filaments can be cleaved, branched, or bundled. Here, we discuss the actin cytoskeleton and its functions. We will examine the current understanding for how the actin cytoskeleton is tethered to adhesion sites. Finally, we will highlight recent studies describing how the actin cytoskeleton at these adhesion sites is remodeled in response to force.
Details
- Title: Subtitle
- Dynamics of the Actin Cytoskeleton at Adhesion Complexes
- Creators
- Nicholas M. Cronin - Roy J. and Lucille A. Carver College of MedicineKris A. DeMali - Roy J. and Lucille A. Carver College of Medicine
- Resource Type
- Journal article
- Publication Details
- Biology (Basel, Switzerland), Vol.11(1), p.52
- DOI
- 10.3390/biology11010052
- PMID
- 35053050
- PMCID
- PMC8773209
- NLM abbreviation
- Biology (Basel)
- ISSN
- 2079-7737
- eISSN
- 2079-7737
- Publisher
- Mdpi
- Number of pages
- 12
- Grant note
- DOI: 10.13039/100000002, name: National Institutes of Health, award: R35GM136291; DOI: 10.13039/100011343, name: Holden Comprehensive Cancer Center, award: P30CA086862
- Language
- English
- Date published
- 01/01/2022
- Academic Unit
- Dermatology; Fraternal Order of Eagles Diabetes Research Center; Biochemistry and Molecular Biology
- Record Identifier
- 9984288726902771
Metrics
18 Record Views