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Regulation of cell adhesion and motility: a novel function of arrestin proteins
Author(s) -
Cleghorn Whitney Marie,
Chen Dong,
Zhang Xi,
Zent Roy,
Gurevich Vsevolod V.
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.824.4
Subject(s) - microbiology and biotechnology , arrestin , fibronectin , cell adhesion , extracellular matrix , signal transduction , motility , g protein coupled receptor , biology , cell adhesion molecule , adhesion , integrin , chemistry , receptor , cell , biochemistry , organic chemistry
Arrestins regulate G protein‐coupled receptors and other signaling proteins. Over 100 arrestin interaction partners have been identified, implicating arrestins in various signaling pathways and cellular functions. The interactions of many proteins (e.g., Src, JNK3, ERK½, Mdm2,etc.) with receptor‐bound arrestin localize these molecules to receptor‐rich membranes. Our recent finding that arrestins bind microtubules and recruit signaling proteins to the cytoskeleton prompted us to investigate whether arrestins affect cell adhesion, motility, and morphology. Here we show that the overexpression of arrestin2 and arrestin3 differentially regulates cell adhesion. Arrestin3 causes a significant reduction in cell adhesion to extracellular matrix protein fibronectin, whereas arrestin2 does not affect it. We also found that overexpression of arrestin2 and arrestin3 dramatically decreases migration, with arrestin2 showing the greatest reduction. Rhodamin‐phalloidin staining revealed that arrestin2 and arrestin3 induce strikingly different changes in cell morphology. Thus, the two non‐visual arrestins differentially regulate cell adhesion, spreading and migration. This is a novel biological role for arrestin proteins. NIH Grants GM77561 (VVG), DK69921 and VA Merit Award (RZ)