Abstract
The composition and organization of the plasma membrane play important functional and regulatory roles in integrin signaling, which direct many physiological and pathological processes, such as development, wound healing, immunity, thrombosis, and cancer metastasis. Membranes are comprised of regions that are thick or thin owing to spontaneous partitioning of long-chain saturated lipids from short-chain polyunsaturated lipids into domains defined as ordered and liquid-disorder domains, respectively. Liquid-ordered domains are typically 100 nm in diameter and sometimes referred to as lipid rafts. We posit that integrin β senses membrane thickness and that mechanical force on the membrane regulates integrin activation through membrane thinning. This review examines what we know about the nature and mechanism of the interaction of integrins with the plasma membrane and its effects on regulating integrins and its binding partners.
Highlights
Biomembranes are a key component of life, as they allow the formation of compartments to provide conditions required for biochemical reactions, and provide an interaction platform for a multitude of key cellular processes
Lipid rafts are involved in integrin-mediated signal transduction pathways initiated by cell adhesion [16,78,79], as well as in integrin clustering at focal adhesions, which regulates integrin activation (38)
ΑVβ3 integrin restricts thymocyte differentiation antigen 1 (Thy-1)/cluster of differentiation 90 (CD90) into nanoclusters, which activates neural signaling via RhoA and Rho-associated protein kinase (ROCK) to induce altered actin dynamics and neurite retraction [98]
Summary
Biomembranes are a key component of life, as they allow the formation of compartments to provide conditions required for biochemical reactions, and provide an interaction platform for a multitude of key cellular processes. In this review we discuss the role of lipid rafts in integrin-mediated cell adhesion and how lipid rafts can affect integrin structure and signaling. Upon activation with extracellular ligands (Figure 3B,C), integrins change from their lowaffinity binding to their high-affinity binding state, which modifies cell adhesion [37]. Whereby the charged lysine (residue 716) snorkels out of the lipid core while hydrophobic residues (residues 717 through 721), in particular leucines, remain immersed in the membrane This NMR structure of the transmembrane domains of the non-covalently-associated integrin αIIbβ in small bicelles revealed that a so-called inner membrane clasp (IMC) stabilizes the integrin heterodimer at the intracellular side, while this role is performed by the ectodomain and oInut.teJ.rMmole. The recruitment of integrins α4β1 and αLβ2 to lipid raft domains occurs
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