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Cells are mechanical living machines that remodel their microenvironment by adhering and generating forces on the extracellular matrix (ECM) using integrin-dependent adhesion sites (IAS). In return, the biochemical and physical nature of the ECM determines cellular behavior and morphology during proliferation, differentiation and migration. IAS come in different shapes and forms. They have specific compositions, morphologies, mechanical and biochemical signaling activities, which serve different cellular functions. Proteomic studies showed that IAS are composed of a large repertoire of proteins that could be linked to different functional activities, including signaling, force-transmission and force-sensing. Thanks to recent technological advances in microscopy and protein engineering, it is now possible to localize single proteins in three dimensions inside IAS, determine their diffusive behaviors, orientations, and how much mechanical force is transmitted across individual components. Here, we review how researchers have used those tools to investigate how IAS components assemble and dynamically interact to produce diverse functions of adhesive structures.
This article was published in the following journal.
Name: Experimental cell research
Integrins are cell adhesion molecules that are composed of an alpha (α) subunit and a beta (β) subunit with affinity for different extracellular membrane components. The integrin family includes 24 ...
Leukocyte adhesion requires β-integrin activation. Resting integrins exist in a bent-closed conformation-i.e., not extended (E) and not high affinity (H)-unable to bind ligand. Fully activated EH int...
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The integrins are a superfamily of transmembrane proteins composed of α and β subunit dimers involved in cell-cell and cell-extracellular matrix interactions. The largest integrin subgroup is integr...
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A group of three different integrin alpha chains (CD11a, CD11b, CD11c) that are associated with an invariant integrin beta-2 chain (CD18 ANTIGENS). The three resulting leukocyte-adhesion molecules (RECEPTORS, LEUKOCYTE ADHESION) are LYMPHOCYTE FUNCTION-ASSOCIATED ANTIGEN-1; MACROPHAGE-1 ANTIGEN; and ANTIGEN, P150,95.
Surface ligands that mediate cell-to-cell adhesion and function in the assembly and interconnection of the vertebrate nervous system. These molecules promote cell adhesion via a homophilic mechanism. These are not to be confused with NEURAL CELL ADHESION MOLECULES, now known to be expressed in a variety of tissues and cell types in addition to nervous tissue.
A membrane glycoprotein and cell adhesion molecule expressed by LEUKOCYTES that contains multiple Ig-like domains. It is a ligand for LFA-1 (integrin alphaLbeta2) and integrin alpha-D/beta-2. Its interaction with LFA-1 may play a role in the PHAGOCYTOSIS of NEUTROPHILS by MACROPHAGES following APOPTOSIS.
Cell adhesion molecules that mediate neuron-neuron adhesion and neuron-astrocyte adhesion. They are expressed on neurons and Schwann cells, but not astrocytes and are involved in neuronal migration, neurite fasciculation, and outgrowth. Ng-CAM is immunologically and structurally distinct from NCAM.
An integrin alpha subunit that primarily associates with INTEGRIN BETA1 or INTEGRIN BETA4 to form laminin-binding heterodimers. Integrin alpha6 has two alternatively spliced isoforms: integrin alpha6A and integrin alpha6B, which differ in their cytoplasmic domains and are regulated in a tissue-specific and developmental stage-specific manner.
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