Abstract
The transmission of extracellular signals to the interior of the cell is a function of plasma membrane receptors, of which the seven transmembrane receptor family is by far the largest and most versatile. Classically, these receptors stimulate heterotrimeric G proteins, which control rates of generation of diffusible second messengers and entry of ions at the plasma membrane. Recent evidence, however, indicates another previously unappreciated strategy used by the receptors to regulate intracellular signaling pathways. They direct the recruitment, activation, and scaffolding of cytoplasmic signaling complexes via two multifunctional adaptor and transducer molecules, β-arrestins 1 and 2. This mechanism regulates aspects of cell motility, chemotaxis, apoptosis, and likely other cellular functions through a rapidly expanding list of signaling pathways.
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Dates
Type | When |
---|---|
Created | 20 years, 4 months ago (April 21, 2005, 5:43 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 9, 2024, 11:35 p.m.) |
Indexed | 1 day, 1 hour ago (Aug. 28, 2025, 8:05 a.m.) |
Issued | 20 years, 4 months ago (April 22, 2005) |
Published | 20 years, 4 months ago (April 22, 2005) |
Published Print | 20 years, 4 months ago (April 22, 2005) |
@article{Lefkowitz_2005, title={Transduction of Receptor Signals by ß-Arrestins}, volume={308}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.1109237}, DOI={10.1126/science.1109237}, number={5721}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Lefkowitz, Robert J. and Shenoy, Sudha K.}, year={2005}, month=apr, pages={512–517} }