Structure, signaling mechanism and regulation of the natriuretic peptide receptor guanylate cyclase.
Structure, signaling mechanism and regulation of the natriuretic peptide receptor guanylate cyclase.
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DOI：
10.1111/j.1742-4658.2011.08083.x
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发表时间：
2011-06
期刊：
影响因子：
--
通讯作者：
Young HS
中科院分区：
文献类型：
--
作者：
Misono KS;Philo JS;Arakawa T;Ogata CM;Qiu Y;Ogawa H;Young HS
心房利钠肽（ANP）和同源B型利钠肽（BNP）是心脏激素，其扩张血管并刺激尿钠排泄和利尿，从而降低血压和血容量。心钠素和脑钠素平衡肾素-血管紧张素-醛固酮和神经激素系统的作用，并在心血管调节中发挥核心作用。这些活性由A型利钠肽受体（NPRA）介导，NPRA是一个单一的跨膜片段，鸟苷酸环化酶（GC）连接的受体，以同型二聚体形式存在。在这里，我们提出了一个概述的结构，可能的氯介导的调节，和信号传导机制的NPRA和其他受体GC。早些时候，我们确定了晶体结构的NPRA细胞外结构域结合和不结合ANP。它们的结构比较揭示了一种新的心钠素诱导的旋转机制发生在质膜区域，显然触发跨膜信号转导。最近，已报道了绿色藻类GC Cyg 12和蓝藻GC Cya 2的二聚催化结构域的晶体结构。这些结构非常类似于由C1和C2亚结构域异二聚体组成的腺苷酸环化酶催化结构域。AC通过Gsα与C2结合并确保C1围绕平行于中心裂隙的轴旋转7°而被激活，从而诱导异二聚体形成催化活性构象。我们推测，在NPRA中，ANP诱导的跨膜结构域的旋转，跨膜螺旋传输，可能会导致类似的旋转在每个二聚GC催化结构域，导致刺激的GC催化活性。
Atrial natriuretic peptide (ANP) and homologous B-type natriuretic peptide (BNP) are cardiac hormones that dilate blood vessels and stimulate natriuresis and diuresis, thereby lowering blood pressure and blood volume. ANP and BNP counterbalance the actions of the renin-angiotensin-aldosterone and neurohormonal systems, and play a central role in cardiovascular regulation. These activities are mediated by the A-type natriuretic peptide receptor (NPRA), a single transmembrane segment, guanylate cyclase (GC) linked receptor that occurs as a homodimer. Here we present an overview of the structure, possible chloride-mediated regulation, and signaling mechanism of the NPRA and other receptor-GCs. Earlier, we determined the crystal structures of the NPRA extracellular domain with and without bound ANP. Their structural comparison has revealed a novel ANP-induced rotation mechanism occurring in the juxtamembrane region that apparently triggers transmembrane signal transduction. More recently, the crystal structures of the dimerized catalytic domain of green algae GC Cyg12 and that of cyanobacter GC Cya2 have been reported. These structures closely resemble that of the adenylate cyclase catalytic domain consisting of C1 and C2 subdomain heterodimer. AC is activated by binding of Gsα to C2 and ensuing 7° rotation of C1 around an axis parallel to the central cleft, thereby inducing the heterodimer into a catalytically active conformation. We speculate that, in the NPRA, the ANP-induced rotation of the juxtamembrane domains, transmitted across the transmembrane helices, may induce a similar rotation in each of the dimerized GC catalytic domains, leading to the stimulation of the GC catalytic activity.
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DOI：
10.1007/bf01726575
发表时间：
1988-09-01
期刊：
KLINISCHE WOCHENSCHRIFT
影响因子：
--
作者：
ANDO, K;UMETANI, N;MARUMO, F
通讯作者：
MARUMO, F
影响因子：
15.9
作者：
HANLEY, MJ;KOKKO, JP
通讯作者：
KOKKO, JP
影响因子：
56.9
作者：
BURNETT, JC;KAO, PC;REEDER, GS
通讯作者：
REEDER, GS
影响因子：
64.8
作者：
CHINKERS, M;GARBERS, DL;SCHULZ, S
通讯作者：
SCHULZ, S
DOI：
10.1152/ajprenal.1996.270.2.f301
发表时间：
1996-02-01
期刊：
AMERICAN JOURNAL OF PHYSIOLOGY-RENAL FLUID AND ELECTROLYTE PHYSIOLOGY
影响因子：
--
作者：
Drummer, C;Franck, W;Goetz, K
通讯作者：
Goetz, K