Integrin and cadherin clusters: A robust way to organize adhesions for cell mechanics

Rishita Changede, Michael Sheetz

Research output: Contribution to journalArticle

21 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)1-12
Number of pages12
JournalBioEssays
Volume39
Issue number1
DOIs
StatePublished - Jan 1 2017
Externally publishedYes

Fingerprint

Cadherins
Mechanics
Cell Adhesion
Integrins
Adhesion
Cell adhesion
Focal Adhesions
Endocytosis
Cytoskeleton
Microscopy
Microscopic examination
Membrane Proteins
Proteins
Binding Sites
Ligands
Molecules

Keywords

  • adhesions
  • cadherin
  • cell forces
  • integrin
  • membrane signaling

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Integrin and cadherin clusters : A robust way to organize adhesions for cell mechanics. / Changede, Rishita; Sheetz, Michael.

In: BioEssays, Vol. 39, No. 1, 01.01.2017, p. 1-12.

Research output: Contribution to journalArticle

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