Indeed, direct activation of integrins via manganese (Mn 2+) or conformation-modulating antibodies appears to enhance cell spreading and adhesion assembly. Integrin receptors undergo conformational activation from a low affinity to high affinity state, and these changes in integrin activity may contribute to the regulation of cell spreading and FA assembly. Because cell spreading, adhesion assembly, and cytoskeletal tension each have been shown to regulate many cellular functions including proliferation, differentiation, and migration, understanding how these processes are regulated is an important question. Conversely, it has been shown that the clustering of integrins required for adhesion assembly is critical to support cell spreading and tension generation. For example, the degree of cell spreading against a micropatterned substrate regulates RhoA activity and cytoskeletal tension, and this cytoskeletal tension is important for adhesion assembly. Each of these processes appears to be linked through several pathways. The binding of integrins to extracellular matrix (ECM) initiates cell adhesion, which can be described as a series of processes including cell spreading against the underlying matrix, assembly of focal adhesions (FAs), and generation of actomyosin-mediated cytoskeletal tension against these adhesions.
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