Ligand Binding to Integrins*

By E. Plow, T. Haas, Li Zhang, J. Loftus, Jeffrey W. Smith. Journal of Biological Chemistry, 2000

1,415 citations recorded by the source corpus.

The “integrin” terminology was applied in a 1987 review article (1) to describe a family of structurally, immunochemically, and functionally related cell-surface heterodimeric receptors, which integrated the extracellular matrix with the intracellular cytoskeleton to mediate cell migration and adhesion. The three original b subunits (b1, b2, and b3) identified have now expanded to eight, and the number of a subunits stands at 17. These subunits interact noncovalently in a restricted manner to form more than 20 family members. The diversity of integrins is expanded further by alternative splicing, post-translational modifications, and interactions with other cell-surface and intracellular molecules (2–4). The number of integrins and the remarkable breadth of their cellular distribution support the statement that the phenotype of virtually every cell is uniquely influenced by its display of integrins. Over the past 13 years, more than 14,000 scientific articles have dealt with various aspects of integrin biology and almost 1,000 have appeared in the Journal of Biological Chemistry. This article examines a central aspect of integrin biology: ligand recognition and the structural basis for this function.

Subfields: Cell Biology, Immunology and Allergy, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/4a90bc2d682ff29ca3ce3ba968011968423ba015

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

In Immunology and Allergy

In Radiology, Nuclear Medicine and Imaging

Citations in the corpus

Functional structure and composition of the extracellular matrix (2003, background): “The latter is also recognized by the α6β4 heterodimer [17,18].”
Probabilistic variable-length segmentation of protein sequences for discriminative motif discovery (DiMotif) and sequence embedding (ProtVecX) (2018, background): “Other known integrin-binding motifs were also among the most significant ones, such as RLD [59], KGD (the binding site for the αIIβ3 integrins [61]), GPR (the binding site for αxβ2 [60]), LDT (the binding site for α4β7 [60]), QIDS (the binding site for α4β1 [60]), DLLEL (the binding site for αvβ6 [6”
INTEGRIN LIGANDS (2006, background): “Moreover, many extracellular matrix and cell surface adhesion proteins bind to multiple integrin receptors (Humphries, 1990; Plow et al., 2000; van der Flier and Sonnenberg, 2001).”
Scatter-factor and semaphorin receptors: cell signalling for invasive growth (2002, background): “Integrin activation is a complex phenomenon that includes conformational changes within their extracellular domains (affinity regulation) and enrichment at discrete sites along the plane of the plasma membrane (avidity regulation”
Integrin structure, activation, and interactions. (2011, background): “Conversely, many extracellular matrix (ECM) and cell surface adhesion proteins bind to multiple integrin receptors (Humphries 2000; Plow et al. 2000; van der Flier and Sonnenberg 2001).”
Syndecan-1 regulates αvβ5 integrin activity in B82L fibroblasts (2006, background): “It has a role in matrix adhesion to VN, FN, SPARC and bone sialoprotein (Plow et al., 2000) and is implicated in the invasion of gliomas and metastatic carcinoma cells (Brooks et al., 1997; Jones et al., 1997; Tonn et al., 1998), the latter especially to bone (De et al., 2003).”