A2 Vertaisarvioitu katsausartikkeli tieteellisessä lehdessä
Cooperation Between Integrins and Growth Factor Receptors in Signaling and Endocytosis
Tekijät: Ivaska J, Heino J
Toimittaja: Schekman, Goldstein, lehmann
Julkaisuvuosi: 2011
Journal: Annual Review of Cell and Developmental Biology
Tietokannassa oleva lehden nimi: ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, VOL 27
Lehden akronyymi: ANNU REV CELL DEV BI
Vuosikerta: 27
Aloitussivu: 291
Lopetussivu: 320
Sivujen määrä: 30
ISBN: 978-0-8243-3127-6
ISSN: 1081-0706
DOI: https://doi.org/10.1146/annurev-cellbio-092910-154017
Tiivistelmä
All multicellular animals express receptors for growth factors (GFs) and extracellular matrix (ECM) molecules. Integrin-type ECM receptors anchor cells to their surroundings and concomitantly activate intracellular signal transduction pathways. The same signaling mechanisms are regulated by GF receptors (GFRs). Recently, intensive research efforts have revealed novel mechanisms describing how the two receptor systems collaborate at many different levels. Integrins can directly bind to GFs and promote their activation. Adhesion receptors also organize signaling platforms and assist GFRs or even activate them via ligand-independent mechanisms. Furthermore, integrins can orchestrate endocytosis and recycling of GFRs. Here, we review the present knowledge about the interplay between integrins and GFRs and discuss recent ideas of how this collaboration may explain some previous controversies in integrin research.
All multicellular animals express receptors for growth factors (GFs) and extracellular matrix (ECM) molecules. Integrin-type ECM receptors anchor cells to their surroundings and concomitantly activate intracellular signal transduction pathways. The same signaling mechanisms are regulated by GF receptors (GFRs). Recently, intensive research efforts have revealed novel mechanisms describing how the two receptor systems collaborate at many different levels. Integrins can directly bind to GFs and promote their activation. Adhesion receptors also organize signaling platforms and assist GFRs or even activate them via ligand-independent mechanisms. Furthermore, integrins can orchestrate endocytosis and recycling of GFRs. Here, we review the present knowledge about the interplay between integrins and GFRs and discuss recent ideas of how this collaboration may explain some previous controversies in integrin research.
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