ArticleProceedings of the National Academy of Sciences of the United States of America2000
Membrane-associated GAIP is a phosphoprotein and can be phosphorylated by clathrin-coated vesicles.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 44 citations in OpenAlex.
- GenPTM: A Generalizable Framework for Protein Post-Translational Modification Information Extraction from the Scientific Literature.Research square · 2026Article
- Review
- Notch signaling regulates the phosphorylation of Akt and survival of lipopolysaccharide-activated macrophages via regulator of G protein signaling 19 (RGS19).Immunobiology · 2014Article
- Modulation of μ-opioid receptor signaling by RGS19 in SH-SY5Y cells.Molecular pharmacology · 2013Article
- Article
- A finer tuning of G-protein signaling through regulated control of RGS proteins.American journal of physiology. Heart and circulatory physiology · 2012Review
- How regulators of G protein signaling achieve selective regulation.Journal of molecular biology · 2007Review
- GIPC recruits GAIP (RGS19) to attenuate dopamine D2 receptor signaling.Molecular biology of the cell · 2004Article
- RGS3 interacts with 14-3-3 via the N-terminal region distinct from the RGS (regulator of G-protein signalling) domain.The Biochemical journal · 2002Article
- Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Phosphorylation of RGS9-1 by an endogenous protein kinase in rod outer segments.The Journal of biological chemistry · 2001Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
Abstract
GAIP (G alpha interacting protein) is a member of the RGS (regulators of G protein signaling) family and accelerates the turnover of GTP bound to Galphai, Galphaq, and Galpha13. There are two pools of GAIP-a soluble and a membrane-anchored pool. The membrane-anchored pool is found on clathrin-coated vesicles (CCVs) and pits in rat liver and AtT-20 pituitary cells. By treatment of a GAIP-enriched rat liver fraction with alkaline phosphatase, we found that membrane-bound GAIP is phosphorylated. By immunoprecipitation carried out on [(32)P]orthophosphate-labeled AtT-20 pituitary cells stably expressing GAIP, (32)P-labeling was associated exclusively with the membrane pool of GAIP. Phosphoamino acid analysis revealed that phosphorylation of GAIP occurred largely on serine residues. Recombinant GAIP could be phosphorylated at its N terminus with purified casein kinase 2 (CK2). It could also be phosphorylated by isolated CCVs in vitro. Phosphorylation was Mn(2+)-dependent, using both purified CK2 and CCVs. Ser-24 was identified as one of the phosphorylation sites. Our results establish that GAIP is phosphorylated and that only the membrane pool is phosphorylated, suggesting that GAIP can be regulated by phosphorylation events taking place at the level of clathrin-coated pits and vesicles.
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