Journal
CURRENT OPINION IN CELL BIOLOGY
Volume 18, Issue 5, Pages 579-586Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.ceb.2006.08.005
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Funding
- NCI NIH HHS [R37 CA031798, R01 CA031798, R01 CA031799, CA31798] Funding Source: Medline
- NHLBI NIH HHS [HL48675, P01 HL048675] Funding Source: Medline
- NIAID NIH HHS [AI72765, R01 AI072765] Funding Source: Medline
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Integrins are cell adhesion molecules that play critical roles in development, wound healing, hemostasis, immunity and cancer. Advances in the past two years have shed light on the structural basis for integrin regulation and signaling, especially on how global conformational changes between bent and extended conformations relate to the inter-domain and intra-domain shape shifting that regulates affinity for ligand. The downward movements of the C-terminal helices of the alpha 1 and beta 1 domains and the swing-out of the hybrid domain play pivotal roles in integrin conformational signaling. Experiments have also shown that integrins transmit bidirectional signals across the plasma membrane by coupling extracellular conformational change with an unclasping and separation of the alpha and beta transmembrane and cytoplasmic domains.
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