The
            <i>mas</i>
            Oncogene as a Neural Peptide Receptor: Expression, Regulation and Mechanism of Action

Mr, Hanley; Wt, Cheung; Hawkins, Phillip T.; Poyner, David R.; Hp, Benton; Blair, Leslie A.C.; Tr, Jackson; Goedert, Michel

doi:10.1002/9780470513927.ch3

Cited by 5 publications

(3 citation statements)

References 47 publications

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“…It is well-established that the proximal portion of ICL3 in many family A GPCRs forms an amphipathic R-helix and that this is important in G-protein coupling (31). Similar features have been noted in family B GPCRs; a study of the GLP-1 receptor concluded that the hydrophobic face of this helix was involved in G-protein contacts (4).…”

Section: Discussionmentioning

confidence: 69%

Diverse Functional Motifs within the Three Intracellular Loops of the CGRP₁ Receptor

et al. 2006

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The CGRP(1) receptor exists as a heterodimeric complex between a single-pass transmembrane accessory protein (RAMP1) and a family B G-protein-coupled receptor (GPCR) called the calcitonin receptor-like receptor (CLR). This study investigated the structural motifs found in the intracellular loops (ICLs) of this receptor. Molecular modeling was used to predict active and inactive conformations of each ICL. Conserved residues were altered to alanine by site-directed mutagenesis. cAMP accumulation, cell-surface expression, agonist affinity, and CGRP-stimulated receptor internalization were characterized. Within ICL1, L147 and particularly R151 were important for coupling to G(s). R151 may interact directly with the G-protein, accessing it following conformational changes involving ICL2 and ICL3. At the proximal end of ICL3, I290 and L294, probably lying on the same face of an alpha helix, formed a G-protein coupling motif. The largest effects on coupling were observed with I290A; additionally, it reduced CGRP affinity and impaired internalization. I290 may interact with TM6 to stabilize the conformation of ICL3, but it could also interact directly with Gs. R314, at the distal end of ICL3, impaired G-protein coupling and to a lesser extent reduced CGRP affinity; it may stabilize the TM6-ICL3 junction by interacting with the polar headgroups of membrane phospholipids. Y215 and L214 in ICL2 are required for cell-surface expression; they form a microdomain with H216 which has the same function. This study reveals similarities between the activation of CLR and other GPCRs in the role of TM6 and ICL3 but shows that other conserved motifs differ in their function.

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Section: Discussionmentioning

confidence: 69%

Diverse Functional Motifs within the Three Intracellular Loops of the CGRP₁ Receptor

et al. 2006

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“…Recently, Santos et al (90) identified the orphan mas receptor as a site for binding ANG- (1-7). The mas receptor, characterized as an oncogene receptor, was shown to influence fetal regulation of cellular differentiation and growth (48). Originally, the mas receptor was considered to be the first ANG II receptor isolated from tissues (57), but other studies soon disproved its participation.…”

Section: Angiotensin-(1-7)mentioning

confidence: 99%

Advances in biochemical and functional roles of angiotensin-converting enzyme 2 and angiotensin-(1–7) in regulation of cardiovascular function

Ferrario

Trask

Jessup

2005

American Journal of Physiology-Heart and Circulatory Physiology

357

317

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Angiotensin-converting enzyme 2 (ACE2) is the first human homologue of ACE to be described. ACE2 is a type I integral membrane protein that functions as a carboxypeptidase, cleaving a single hydrophobic/basic residue from the COOH-terminus of its substrates. Because ACE2 efficiently hydrolyzes the potent vasoconstrictor angiotensin II to angiotensin (1-7), this has changed our overall perspective about the classical view of the renin angiotensin system in the regulation of hypertension and heart and renal function, because it represents the first example of a feedforward mechanism directed toward mitigation of the actions of angiotensin II. This paper reviews the new data regarding the biochemistry of angiotensin-(1-7)-forming enzymes and discusses key findings such as the elucidation of the regulatory mechanisms participating in the expression of ACE2 and angiotensin-(1-7) in the control of the circulation.

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“…For many years, the work of Ferrario and Chappel 4 provided evidence that Ang-(1-7) operated in the central nervous system, as well as in the peripheral circulation to produce effects that were, in general, opposite to that of Ang II. Recently, the discovery that Ang-(1-7) binds to a specific membrane receptor, the mas receptor, [5][6][7] suggests that this metabolite may play a regulatory role in cell signaling and organ function. Clearly, the balance between the classic ACE and ACE2 will determine the physiological effect of activation of the RAS.…”

mentioning

confidence: 99%

Angiotensin-Converting Enzyme 2

Zucker

2008

Circulation Research

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The mas Oncogene as a Neural Peptide Receptor: Expression, Regulation and Mechanism of Action

Cited by 5 publications

References 47 publications

Diverse Functional Motifs within the Three Intracellular Loops of the CGRP₁ Receptor

Diverse Functional Motifs within the Three Intracellular Loops of the CGRP₁ Receptor

Advances in biochemical and functional roles of angiotensin-converting enzyme 2 and angiotensin-(1–7) in regulation of cardiovascular function

Angiotensin-Converting Enzyme 2

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The mas Oncogene as a Neural Peptide Receptor: Expression, Regulation and Mechanism of Action

Cited by 5 publications

References 47 publications

Diverse Functional Motifs within the Three Intracellular Loops of the CGRP1 Receptor

Diverse Functional Motifs within the Three Intracellular Loops of the CGRP1 Receptor

Advances in biochemical and functional roles of angiotensin-converting enzyme 2 and angiotensin-(1–7) in regulation of cardiovascular function

Angiotensin-Converting Enzyme 2

Contact Info

Product

Resources

About

Diverse Functional Motifs within the Three Intracellular Loops of the CGRP₁ Receptor

Diverse Functional Motifs within the Three Intracellular Loops of the CGRP₁ Receptor