دورية أكاديمية

Conserved motifs in somatostatin, D2-dopamine, and alpha 2B-adrenergic receptors for inhibiting the Na-H exchanger, NHE1.

التفاصيل البيبلوغرافية
العنوان: Conserved motifs in somatostatin, D2-dopamine, and alpha 2B-adrenergic receptors for inhibiting the Na-H exchanger, NHE1.
المؤلفون: Lin CY; University of California, San Francisco, San Francisco, California 94143, USA., Varma MG, Joubel A, Madabushi S, Lichtarge O, Barber DL
المصدر: The Journal of biological chemistry [J Biol Chem] 2003 Apr 25; Vol. 278 (17), pp. 15128-35. Date of Electronic Publication: 2003 Feb 03.
نوع المنشور: Journal Article; Research Support, U.S. Gov't, P.H.S.
اللغة: English
بيانات الدورية: Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
أسماء مطبوعة: Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
مواضيع طبية MeSH: Receptors, Cell Surface/*chemistry , Sodium-Hydrogen Exchangers/*antagonists & inhibitors, Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Conserved Sequence ; Membrane Proteins ; Rats ; Receptors, Adrenergic, alpha-2/chemistry ; Receptors, Adrenergic, alpha-2/metabolism ; Receptors, Cell Surface/metabolism ; Receptors, Dopamine D2/chemistry ; Receptors, Dopamine D2/metabolism ; Receptors, Somatostatin/chemistry ; Receptors, Somatostatin/metabolism ; Sequence Alignment ; Signal Transduction ; Sodium-Hydrogen Exchangers/metabolism
مستخلص: Receptor subtypes within families of G protein-coupled receptors that are activated by similar ligands can regulate distinct intracellular effectors. We identified conserved motifs within intracellular domains 2 and 3 of selective subtypes of several G protein-coupled receptor families that confer coupling to the Na-H exchanger, NHE1. A T(s,p)V motif within intracellular domain 2 and a QQ(r) motif within intracellular domain 3 are shared by the somatostatin receptor subtypes SSTR1, -3, and -4, which couple to the inhibition of NHE1, but not by SSTR2 and -5, which do not signal to NHE1. Only the collective substitution of cognate SSTR2 residues with these two motifs conferred the ability of mutant SSTR2 to inhibit NHE1. Both motifs are present in D(2)-dopamine receptors, which inhibit NHE1, and in alpha(2B)-adrenergic receptors, which couple to the inhibition of NHE1, but not in alpha(2A)-adrenergic receptors, which do not regulate NHE1. These findings indicate that motifs shared by different subfamilies of G protein-coupled receptors, but not necessarily by receptor subtypes within a subfamily, can confer coupling to a common effector.
معلومات مُعتمدة: DK40259 United States DK NIDDK NIH HHS; T32DE07204 United States DE NIDCR NIH HHS
المشرفين على المادة: 0 (Membrane Proteins)
0 (Receptors, Adrenergic, alpha-2)
0 (Receptors, Cell Surface)
0 (Receptors, Dopamine D2)
0 (Receptors, Somatostatin)
0 (Sodium-Hydrogen Exchangers)
0 (growth factor-activatable Na-H exchanger NHE-1)
0 (somatostatin receptor 3)
0 (somatostatin receptor subtype-4)
تواريخ الأحداث: Date Created: 20030205 Date Completed: 20030716 Latest Revision: 20210209
رمز التحديث: 20240627
DOI: 10.1074/jbc.M212315200
PMID: 12566440
قاعدة البيانات: MEDLINE
الوصف
تدمد:0021-9258
DOI:10.1074/jbc.M212315200