Integrin and cadherin clusters: A robust way to organize adhesions for cell mechanics. (8th December 2016)

• Record Type: Journal Article
• Authors: Changede, Rishita; Sheetz, Michael
• Is Part Of: BioEssays. Volume 39:Number 1(2017:Jan.)
• Page Start: 1
• Page End: 12
• Publication Date: 2016-12-08
• Subjects: adhesions -- cadherin -- cell forces -- integrin -- membrane signaling; Molecular biology -- Periodicals; Cytology -- Periodicals; Developmental biology -- Periodicals; 572.8
• DOI: 10.1002/bies.201600123
• Languages: English
• ISSNs: 0265-9247

Abstract

Abstract : Recent studies at the nanometer scale have revealed that relatively uniform clusters of adhesion proteins (50–100 nm) constitute the modular units of cell adhesion sites in both cell‐matrix and cell‐cell adhesions. Super resolution microscopy and membrane protein diffusion studies both suggest that even large focal adhesions are formed of 100 nm clusters that are loosely aggregated. Clusters of 20–50 adhesion molecules (integrins or cadherins) can support large forces through avidity binding interactions but can also be disassembled or endocytosed rapidly. Assembly of the clusters of integrins is force‐independent and involves gathering integrins at ligand binding sites where they are stabilized by cytoplasmic adhesion proteins that crosslink the integrin cytoplasmic tails plus connect the clusters to the cell cytoskeleton. Cooperative‐signaling events can occur in a single cluster without cascading to other clusters. Thus, the clusters appear to be very important elements in many cellular processes and can be considered as a critical functional module. Abstract : Adhesion proteins, both integrins and cadherins, form clusters of fairly uniform size. Clusters form prior to mechanosensing as a result of adhesion protein activation and enable strong mechanical bonds to the cytoskeleton that are dynamic. Mechano signaling and mechanotransduction processes occur locally at these spatially segregated sites.