Genetic and cell biological analysis of integrin outside-in signaling.

By K. Legate, S. Wickström, R. Fässler. Genes & Development, 2009

822 citations recorded by the source corpus.

Integrins are cell surface transmembrane receptors that recognize and bind to extracellular matrix proteins and counter receptors. Binding of activated integrins to their ligands induces a vast number of structural and signaling changes within the cell. Large, multimolecular complexes assemble onto the cytoplasmic tails of activated integrins to engage and organize the cytoskeleton, and activate signaling pathways that ultimately lead to changes in gene expression. Additionally, integrin-mediated signaling intersects with growth factor-mediated signaling through various levels of cross-talk. This review discusses recent work that has tremendously broadened our understanding of the complexity of integrin-mediated signaling.

Subfields: Immunology and Allergy, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/ec424105384c7fa30304619ab0d66e27b35dbff9

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Citations in the corpus

Comprehending crystalline β-carotene accumulation by comparing engineered cell models and the natural carotenoid-rich system of citrus (2011, neutral): “The transcript abundance was normalized against peanut Ubiquitin (Luo et al. , 2005) transcript levels.”
Integrins (2009, background): “The scope of this review does not include these events, but readers are referred to recent excellent reviews on this subject (Askari et al. 2009; Gahmberg et al. 2009; Larjava et al. 2008; Legate et al. 2009; Luo and Springer 2006).”
Extracellular matrix: A dynamic microenvironment for stem cell niche (2014, neutral): “proliferation, survival and differentiation [40].”
Extracellular matrix and cell signalling: the dynamic cooperation of integrin, proteoglycan and growth factor receptor. (2011, background): “2000) and inﬂammation (Li & Vlodavsky 2009), where heparanase has been investigated as a therapeutic target for new treatments.”
Integrin Structure and Function (2010, background): “Tensin also interfaces with signaling pathways through binding tyrosine-phosphorylated FAK, p130Cas, epidermal growth factor receptor (EGFR), the Akt kinase PDK1, and the RhoGAPs (Legate et al. 2009).”