期刊
MOLECULAR AND CELLULAR ENDOCRINOLOGY
卷 321, 期 2, 页码 112-122出版社
ELSEVIER IRELAND LTD
DOI: 10.1016/j.mce.2010.02.027
关键词
Follicle-stimulating hormone receptor; Dominant negative receptor; Dimerization; Intracellular trafficking; Endoplasmic reticulum; Decoy
资金
- FOFOI-IMSS, Mexico [2006/1A/I/008]
- CONACyT, Mexico [86881]
- National Institutes of Health, Bethesda, MD, USA [HD-19899, RR-00163, HD-18185, TW/HD-00668, HD-18407]
- Fundacion-IMSS, Mexico
Current evidence indicates that G protein-coupled receptors form dimers that may affect biogenesis and membrane targeting of the complexed receptors We here analyzed whether expression-deficient follicle-stimulating hormone receptor (FSHR) mutants exert dominant negative actions on wild-type FSHR cell surface membrane expression Co-transfection of constant amounts of wild-type receptor cDNA and increasing quantities of mutant (R556A or R618A) FSHR cDNAs progressively decreased agonist-stimulated cAMP accumulation, [I-125]-FSH binding, and plasma membrane expression of the mature wild-type FSHR species Co-transfection of wild-type FSHR fragments involving transmembrane domains 5-6, or transmembrane domain 7 and/or the carboxyl-terminus specifically rescued wild-type FSHR expression from the transdominant inhibition by the mutants Mutant FSHRs also inhibited function of the luteinizing hormone receptor but not that of the thyrotropin receptor or non-related receptors. Defective intracellular transport and/or interference with proper maturation due to formation of misfolded mutant wild-type receptor complexes may explain the negative effects provoked by the altered FSHRs (C) 2010 Elsevier Ireland Ltd. All rights reserved
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