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18 April 2024 |
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G-protein signaling through tubby proteins | | S Santagata
; T J Boggon
; C L Baird
; C A Gomez
; J Zhao
; W S Shan
; D G Myszka
; L Shapiro
; | | Date: |
15 Jun 2001 | | Journal: | Science, 292 (5524), 2041-50 | | Abstract: | Dysfunction of the tubby protein results in maturity-onset obesity in mice. Tubby has been implicated as a transcription regulator, but details of the molecular mechanism underlying its function remain unclear. Here we show that tubby functions in signal transduction from heterotrimeric GTP-binding protein (G protein)-coupled receptors. Tubby localizes to the plasma membrane by binding phosphatidylinositol 4,5-bisphosphate through its carboxyl terminal "tubby domain." X-ray crystallography reveals the atomic-level basis of this interaction and implicates tubby domains as phosphorylated-phosphatidyl- inositol binding factors. Receptor-mediated activation of G protein alphaq (Galphaq) releases tubby from the plasma membrane through the action of phospholipase C-beta, triggering translocation of tubby to the cell nucleus. The localization of tubby-like protein 3 (TULP3) is similarly regulated. These data suggest that tubby proteins function as membrane-bound transcription regulators that translocate to the nucleus in response to phosphoinositide hydrolysis, providing a direct link between G-protein signaling and the regulation of gene expression. | | Source: | PubMed, pmid11375483 doi: 10.1126/science.1061233 | | Services: | Forum | Review | Favorites | |
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