دورية أكاديمية
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Human Melanocortin-2 Receptor: Identifying a Role for Residues in the TM4, EC2, and TM5 Domains in Activation and Trafficking as a Result of Co-Expression with the Accessory Protein, Mrap1 in Chinese Hamster Ovary Cells.

التفاصيل البيبلوغرافية
العنوان: Human Melanocortin-2 Receptor: Identifying a Role for Residues in the TM4, EC2, and TM5 Domains in Activation and Trafficking as a Result of Co-Expression with the Accessory Protein, Mrap1 in Chinese Hamster Ovary Cells.
المؤلفون: Davis PV; Department of Biological Sciences, University of Denver, Denver, CO 80210, USA., Shaughnessy CA; Department of Biological Sciences, University of Denver, Denver, CO 80210, USA., Dores RM; Department of Biological Sciences, University of Denver, Denver, CO 80210, USA.
المصدر: Biomolecules [Biomolecules] 2022 Oct 04; Vol. 12 (10). Date of Electronic Publication: 2022 Oct 04.
نوع المنشور: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: MDPI Country of Publication: Switzerland NLM ID: 101596414 Publication Model: Electronic Cited Medium: Internet ISSN: 2218-273X (Electronic) Linking ISSN: 2218273X NLM ISO Abbreviation: Biomolecules Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI, 2011-
مواضيع طبية MeSH: Receptor, Melanocortin, Type 2*/genetics , Receptor, Melanocortin, Type 2*/chemistry , Receptor, Melanocortin, Type 2*/metabolism , Adrenocorticotropic Hormone*/metabolism, Cricetinae ; Humans ; Mice ; Animals ; Cricetulus ; CHO Cells ; Xenopus/metabolism ; Alanine
مستخلص: Human melanocortin-2 receptor (hMC2R) co-expressed with the accessory protein mouse (m)MRAP1 in Chinese Hamster Ovary (CHO) cells has been used as a model system to investigate the activation and trafficking of hMC2R. A previous study had shown that the N-terminal domain of mMRAP1 makes contact with one of the extracellular domains of hMC2R to facilitate activation of hMC2R. A chimeric receptor paradigm was used in which the extracellular domains of hMC2R were replaced with the corresponding domains from Xenopus tropicalis MC1R, a receptor that does not interact with MRAP1, to reveal that EC2 (Extracellular domain 2) is the most likely contact site for hMC2R and mMRAP1 to facilitate activation of the receptor following an ACTH binding event. Prior to activation, mMRAP1 facilitates the trafficking of hMC2R from the ER to the plasma membrane. This process is dependent on the transmembrane domain (TM) of mMRAP1 making contact with one or more TMs of hMC2R. A single alanine substitution paradigm was used to identify residues in TM4 (i.e., I 163 , M 165 ), EC2 (F 167 ), and TM5 (F 178 ) that play a role in the trafficking of hMC2R to the plasma membrane. These results provide further clarification of the activation mechanism for hMC2R.
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فهرسة مساهمة: Keywords: ACTH; MRAP1; activation; human MC2R; trafficking
المشرفين على المادة: 0 (Receptor, Melanocortin, Type 2)
9002-60-2 (Adrenocorticotropic Hormone)
OF5P57N2ZX (Alanine)
تواريخ الأحداث: Date Created: 20221027 Date Completed: 20221028 Latest Revision: 20221222
رمز التحديث: 20240829
مُعرف محوري في PubMed: PMC9599514
DOI: 10.3390/biom12101422
PMID: 36291631
قاعدة البيانات: MEDLINE
الوصف
تدمد:2218-273X
DOI:10.3390/biom12101422