Mechanosensitivity and compositional dynamics of cell–matrix adhesions. (17th May 2013)
- Record Type:
- Journal Article
- Title:
- Mechanosensitivity and compositional dynamics of cell–matrix adhesions. (17th May 2013)
- Main Title:
- Mechanosensitivity and compositional dynamics of cell–matrix adhesions
- Authors:
- Schiller, Herbert B
Fässler, Reinhard - Abstract:
- Abstract : Cells perceive information about the biochemical and biophysical properties of their tissue microenvironment through integrin‐mediated cell–matrix adhesions, which connect the cytoskeleton with the extracellular matrix and thereby allow cohesion and long‐range mechanical connections within tissues. The formation of cell–matrix adhesions and integrin signalling involves the dynamic recruitment and assembly of an inventory of proteins, collectively termed the 'adhesome', at the adhesive site. The recruitment of some adhesome proteins, most notably the Lin11‐, Isl1‐ and Mec3‐domain‐containing proteins, depends on mechanical tension generated by myosin II‐mediated contractile forces exerted on cell–matrix adhesions. When exposed to force, mechanosensitive adhesome proteins can change their conformation or expose cryptic‐binding sites leading to the recruitment of proteins, rearrangement of the cytoskeleton, reinforcement of the adhesive site and signal transduction. Biophysical methods and proteomics revealed force ranges within the adhesome and cytoskeleton, and also force‐dependent changes in adhesome composition. In this review, we provide an overview of the compositional dynamics of cell–matrix adhesions, discuss the most prevalent functional domains in adhesome proteins and review literature and concepts about mechanosensing mechanisms that operate at the adhesion site. Abstract : This review provides an overview of the compositional dynamics of cell–matrixAbstract : Cells perceive information about the biochemical and biophysical properties of their tissue microenvironment through integrin‐mediated cell–matrix adhesions, which connect the cytoskeleton with the extracellular matrix and thereby allow cohesion and long‐range mechanical connections within tissues. The formation of cell–matrix adhesions and integrin signalling involves the dynamic recruitment and assembly of an inventory of proteins, collectively termed the 'adhesome', at the adhesive site. The recruitment of some adhesome proteins, most notably the Lin11‐, Isl1‐ and Mec3‐domain‐containing proteins, depends on mechanical tension generated by myosin II‐mediated contractile forces exerted on cell–matrix adhesions. When exposed to force, mechanosensitive adhesome proteins can change their conformation or expose cryptic‐binding sites leading to the recruitment of proteins, rearrangement of the cytoskeleton, reinforcement of the adhesive site and signal transduction. Biophysical methods and proteomics revealed force ranges within the adhesome and cytoskeleton, and also force‐dependent changes in adhesome composition. In this review, we provide an overview of the compositional dynamics of cell–matrix adhesions, discuss the most prevalent functional domains in adhesome proteins and review literature and concepts about mechanosensing mechanisms that operate at the adhesion site. Abstract : This review provides an overview of the compositional dynamics of cell–matrix adhesions and discusses the most prevalent functional domains in adhesome proteins. It also reviews the current literature and concepts about mechanosensing mechanisms that operate at the adhesion site. … (more)
- Is Part Of:
- EMBO reports. Volume 14:Number 6(2013)
- Journal:
- EMBO reports
- Issue:
- Volume 14:Number 6(2013)
- Issue Display:
- Volume 14, Issue 6 (2013)
- Year:
- 2013
- Volume:
- 14
- Issue:
- 6
- Issue Sort Value:
- 2013-0014-0006-0000
- Page Start:
- 509
- Page End:
- 519
- Publication Date:
- 2013-05-17
- Subjects:
- adhesome -- focal adhesion -- quantitative proteomics -- integrins -- extracellular matrix
Molecular biology -- Periodicals
Molecular Biology -- Periodicals
Molecular biology
Periodicals
572.8 - Journal URLs:
- http://www.embo-reports.oupjournals.org/ ↗
http://onlinelibrary.wiley.com/ ↗
http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=1469-221x;screen=info;ECOIP ↗ - DOI:
- 10.1038/embor.2013.49 ↗
- Languages:
- English
- ISSNs:
- 1469-221X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3733.086000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 2839.xml