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Amino acids in the COOH-terminal region of the oxytocin receptor third intracellular domain are important for receptor function

American journal of physiology: endocrinology and metabolism, 2007-04, Vol.292 (4), p.E977-E984 [Peer Reviewed Journal]

Copyright American Physiological Society Apr 2007 ;ISSN: 0193-1849 ;EISSN: 1522-1555 ;DOI: 10.1152/ajpendo.00531.2005 ;PMID: 17148753 ;CODEN: AJPMD9

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  • Title:
    Amino acids in the COOH-terminal region of the oxytocin receptor third intracellular domain are important for receptor function
  • Author: Zhong, Miao ; Parish, Bridgette ; Murtazina, Dilyara A ; Ku, Chun-Ying ; Sanborn, Barbara M
  • Subjects: Alanine ; Amino Acid Sequence ; Amino Acid Substitution ; Amino acids ; Arginine ; Biochemistry ; Cell Line ; Cells ; Extracellular Signal-Regulated MAP Kinases - metabolism ; Gene Deletion ; Humans ; Intracellular Membranes - metabolism ; Kinases ; Molecular Sequence Data ; Mutation ; Phosphatidylinositols - metabolism ; Phosphorylation ; Protein Structure, Tertiary ; Proteins ; Receptors, Oxytocin - genetics ; Receptors, Oxytocin - metabolism ; Receptors, Vasopressin - genetics ; Recombinant Fusion Proteins - metabolism ; Vasopressins - pharmacology
  • Is Part Of: American journal of physiology: endocrinology and metabolism, 2007-04, Vol.292 (4), p.E977-E984
  • Description: 1 Department of Biomedical Sciences, Colorado State University, Fort Collins, Colorado; and 2 Department of Biochemistry, University of Texas Medical School, Houston, Texas Submitted 1 November 2005 ; accepted in final form 19 November 2006 Previously, residue K6.30 in the COOH-terminal region of the third intracellular domain (3iC) of the oxytocin (OT) receptor (OTR) was identified as important for receptor function leading to phospholipase C activation in both OTR and the vasopressin V 2 receptor (V 2 R) chimera V 2 ROTR3iC. Substitution of either A6.28K or V6.30K in wild-type V 2 R did not recapitulate the increase in phosphatidylinositide (PI) turnover observed in V 2 ROTR3iC. Hence, the role of K6.30 may be context-specific. Deletion of two NH 2 -terminal OTR3iC segments in the V 2 ROTR3iC chimera did not diminish vasopressin-stimulated PI turnover, whereas deletion of RVSSVKL (residues 6.19–6.25) reduced receptor expression. Deletion of this sequence in wild-type OTR reduced expression by 50% without affecting affinity for [ 3 H]OT. This OTR mutant was unable to activate PI turnover or extracellular signal-regulated kinase 1/2 phosphorylation. The effects of alanine substitution for individual residues in RVSSVKL indicated differential importance for OTR function. The R6.19A substitution lost high-affinity sites for [ 3 H]OT and the ability to stimulate PI turnover. Affinity for [ 3 H]OT and membrane expression was not affected by any other substitutions. OTR-V6.20A and OTR-K6.24A mutants functioned as well as wild-type OTR, whereas OTR S6.21A, S6.22A, and V6.23A mutants exhibited impaired abilities to activate PI turnover (20–40% of OTR), and the OTR-L6.25A mutant exhibited constitutive activity. In conclusion, specific amino acids in the RVSSVKL segment in the COOH-terminal region of the third intracellular domain of OTR influence the ability of OTR to activate G protein-mediated actions. vasopressin type II receptor; G protein; phospholipase C; extracellular signal-regulated protein kinase-1/2 Address for reprint requests and other correspondence: B. M. Sanborn, Dept. of Biomedical Sciences, 102 Physiology Campus Delivery 1680, Colorado State Univ., Fort Collins, CO 80523 (e-mail: Barbara.Sanborn{at}colostate.edu )
  • Publisher: United States: American Physiological Society
  • Language: English
  • Identifier: ISSN: 0193-1849
    EISSN: 1522-1555
    DOI: 10.1152/ajpendo.00531.2005
    PMID: 17148753
    CODEN: AJPMD9
  • Source: Geneva Foundation Free Medical Journals
    MEDLINE
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