The 5-Hydroxytryptamine(4a) Receptor Is Palmitoylated at Two Different Sites, and Acylation Is Critically Involved in Regulation of Receptor Constitutive Activity
Open Access
- 1 January 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (4) , 2534-2546
- https://doi.org/10.1074/jbc.m106529200
Abstract
No abstract availableKeywords
This publication has 55 references indexed in Scilit:
- Acylation of Gα13is important for its interaction with thrombin receptor, transforming activity and actin stress fiber formationFEBS Letters, 2000
- A cysteine-11 to serine mutant of Gα12impairs activation through the thrombin receptorFEBS Letters, 1998
- Cloning, expression and pharmacology of the mouse 5‐HT4L receptorFEBS Letters, 1996
- The Cubic Ternary Complex Receptor-Occupancy Model III. Resurrecting EfficacyJournal of Theoretical Biology, 1996
- Palmitoylation: a post-translational modification that regulates signalling from G-protein coupled receptorsBiochemistry and Cell Biology, 1996
- Agonist Stimulation Increases the Turnover Rate of β2AR-Bound Palmitate and Promotes Receptor DepalmitoylationBiochemistry, 1996
- Protein Modification: Palmitoylation in G-protein signaling pathwaysCurrent Biology, 1995
- Desensitization, phosphorylation and palmitoylation of the human dopamine D1 receptorEuropean Journal of Pharmacology: Molecular Pharmacology, 1994
- The α‐subunits of G‐proteins G12 and G13 are palmitoylated, but not amidically myristoylatedFEBS Letters, 1994
- Fatty acylation of proteinsBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1989