integrin binding

Definition

Target type: molecularfunction

Binding to an integrin. [GOC:ceb]

Integrin binding is a crucial molecular interaction that mediates cell-cell and cell-extracellular matrix (ECM) adhesion. Integrins are transmembrane receptors that play vital roles in diverse cellular processes, including cell migration, proliferation, differentiation, and survival. The molecular function of integrin binding involves a multi-step process that begins with the recognition and binding of specific ligands by the integrin ectodomain. These ligands can be ECM proteins such as collagen, fibronectin, laminin, and vitronectin, or cell surface proteins on neighboring cells. Upon ligand binding, the integrin undergoes a conformational change, shifting from an inactive to an active state. This conformational change exposes the integrin cytoplasmic domain, enabling it to interact with intracellular signaling molecules. These intracellular signaling molecules, such as focal adhesion kinase (FAK) and talin, then relay signals to the cytoskeleton, leading to the assembly of focal adhesions. Focal adhesions are highly organized protein complexes that connect the integrin receptors to the actin cytoskeleton. These connections provide structural support for cells and enable them to exert force on their environment. Integrin binding also plays a role in regulating intracellular signaling pathways, influencing cell behavior and fate. For example, integrin signaling can activate pathways involved in cell growth, survival, and differentiation, while also regulating pathways involved in apoptosis. The intricate interplay between integrin binding, intracellular signaling, and the cytoskeleton highlights the multifaceted role of integrins in maintaining cell homeostasis and orchestrating various cellular processes.'
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Proteins (47)

Compounds (1,955)