Palmitoylation of luteinizing hormone/human choriogonadotropin receptors in transfected cells. Abolition of palmitoylation by mutation of Cys-621 and Cys-622 residues in the cytoplasmic tail increases ligand-induced internalization of the receptor.
Open Access
- 1 December 1994
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 269 (48) , 30651-30658
- https://doi.org/10.1016/s0021-9258(18)43863-x
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Evidence for monomeric and oligomeric hormone-binding domains in affinity-purified gonadotropin receptor from rat ovary.Proceedings of the National Academy of Sciences, 1989
- Fatty acyl-coenzyme a is required for budding of transport vesicles from Golgi cisternaeCell, 1989
- Lutropin-Choriogonadotropin Receptor: An Unusual Member of the G Protein-Coupled Receptor FamilyScience, 1989
- Two adjacent cysteine residues in the C‐terminal cytoplasmic fragment of bovine rhodopsin are palmitylatedFEBS Letters, 1988
- Evidence That Dissociation, Not Intracellular Degradation, is the Major Pathway for Removal of Receptor-bound 125I-Human Chorionic Gonadotropin in Cultured Rat Luteal CellsBiology of Reproduction, 1985
- Identification of the NH2‐terminal blocking group of calcineurin B as myristic acidFEBS Letters, 1982
- The transforming proteins of Rous sarcoma virus, Harvey sarcoma virus and Abelson virus contain tightly bound lipidPublished by Elsevier ,1982
- Glycoprotein Hormones: Structure and FunctionAnnual Review of Biochemistry, 1981
- LIGAND: A versatile computerized approach for characterization of ligand-binding systemsAnalytical Biochemistry, 1980
- [7] Assay of cyclic nucleotides by receptor protein binding displacementPublished by Elsevier ,1974