Stop that cell! Beta-arrestin-dependent chemotaxis: a tale of localized actin assembly and receptor desensitization.
Beta-arrestins have recently emerged as key regulators of directed cell migration or chemotaxis. Given their traditional role as mediators of receptor desensitization, one theory is that beta-arrestins contribute to cell polarity during chemotaxis by quenching the signal at the trailing edge of the cell. A second theory is that they scaffold signaling molecules involved in cytoskeletal reorganization to promote localized actin assembly events leading to the formation of a leading edge. This review addresses both models. It discusses studies demonstrating the involvement of beta-arrestins in chemotaxis both in vivo and in vitro as well as recent evidence that beta-arrestins directly bind and regulate proteins involved in actin reorganization.
DeFea
Kathryn A
KA
Division of Biomedical Sciences and Cell, Molecular, and Developmental Biology Program, University of California, Riverside, California 92521, USA. katied@ucr.edu.
D000199:Actins / Q000096:biosynthesis* / Q000502:physiology*; D000818:Animals; D019390:Arrestins / Q000502:physiology*; D002630:Chemotactic Factors / Q000502:physiology; D002633:Chemotaxis / Q000502:physiology*; D002634:Chemotaxis, Leukocyte / Q000502:physiology; D006801:Humans; D011956:Receptors, Cell Surface / Q000502:physiology; D000071557:beta-Arrestins
D000199:Actins; D019390:Arrestins; D002630:Chemotactic Factors; D011956:Receptors, Cell Surface; D000071557:beta-Arrestins