Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Science 15 May 2009:
Vol. 324. no. 5929, pp. 895 - 899
DOI: 10.1126/science.1163865

Review

The Tail of Integrins, Talin, and Kindlins

Markus Moser,1,* Kyle R. Legate,1,* Roy Zent,2 Reinhard Fässler1

Integrins are transmembrane cell–adhesion molecules that carry signals from the outside to the inside of the cell and vice versa. Like other cell surface receptors, integrins signal in response to ligand binding; however, events within the cell can also regulate the affinity of integrins for ligands. This feature is important in physiological situations such as those in blood, in which cells are always in close proximity to their ligands, yet cell-ligand interactions occur only after integrin activation in response to specific external cues. This review focuses on the mechanisms whereby two key proteins, talin and the kindlins, regulate integrin activation by binding the tails of integrin-β subunits.

1 Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
2 Division of Nephrology, Department of Medicine, Vanderbilt Medical Center and Veterans Affairs Hospital, Nashville, TN 37232, USA.

* These authors contributed equally to this work.

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
{beta}1 integrin is necessary for ureteric bud branching morphogenesis and maintenance of collecting duct structural integrity.
X. Zhang, G. Mernaugh, D.-H. Yang, L. Gewin, M. B. Srichai, R. C. Harris, J. M. Iturregui, R. D. Nelson, D. E. Kohan, D. Abrahamson, et al. (2009)
Development 136, 3357-3366
   Abstract »    Full Text »    PDF »
Loss-of-Function FERMT1 Mutations in Kindler Syndrome Implicate a Role for Fermitin Family Homolog-1 in Integrin Activation.
J. E. Lai-Cheong, M. Parsons, A. Tanaka, S. Ussar, A. P. South, S. Gomathy, J. B. Mee, J.-B. Barbaroux, T. Techanukul, N. Almaani, et al. (2009)
Am. J. Pathol. 175, 1431-1441
   Abstract »    Full Text »    PDF »
Loss of Kindlin-3 in LAD-III eliminates LFA-1 but not VLA-4 adhesiveness developed under shear flow conditions.
E. Manevich-Mendelson, S. W. Feigelson, R. Pasvolsky, M. Aker, V. Grabovsky, Z. Shulman, S. S. Kilic, M. A. Rosenthal-Allieri, S. Ben-Dor, A. Mory, et al. (2009)
Blood 114, 2344-2353
   Abstract »    Full Text »    PDF »
A Sulfilimine Bond Identified in Collagen IV.
R. Vanacore, A.-J. L. Ham, M. Voehler, C. R. Sanders, T. P. Conrads, T. D. Veenstra, K. B. Sharpless, P. E. Dawson, and B. G. Hudson (2009)
Science 325, 1230-1234
   Abstract »    Full Text »    PDF »



To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)