Advances in second messenger and phosphoprotein research最新文献_第2页

L-type calcium channel modulation. l型钙通道调制。

Advances in second messenger and phosphoprotein research Pub Date : 1999-01-01 DOI: 10.1016/s1040-7952(99)80009-3

A C Dolphin

引用次数: 46

Modulation of ion channels by protein phosphorylation. How the brain works. 蛋白磷酸化对离子通道的调节。大脑是如何工作的。

Advances in second messenger and phosphoprotein research Pub Date : 1999-01-01 DOI: 10.1016/s1040-7952(99)80003-2

I B Levitan

引用次数: 132

Regulation of ligand-gated ion channels by protein phosphorylation. 配体门控离子通道的蛋白磷酸化调控。

Advances in second messenger and phosphoprotein research Pub Date : 1999-01-01 DOI: 10.1016/s1040-7952(99)80005-6

S L Swope, S J Moss, L A Raymond, R L Huganir

{"title":"Regulation of ligand-gated ion channels by protein phosphorylation.","authors":"S L Swope, S J Moss, L A Raymond, R L Huganir","doi":"10.1016/s1040-7952(99)80005-6","DOIUrl":"https://doi.org/10.1016/s1040-7952(99)80005-6","url":null,"abstract":"<p><p>The studies discussed in this review demonstrate that phosphorylation is an important mechanism for the regulation of ligand-gated ion channels. Structurally, ligand-gated ion channels are heteromeric proteins comprised of homologous subunits. For both the AChR and the GABA(A) receptor, each subunit has a large extracellular N-terminal domain, four transmembrane domains, a large intracellular loop between transmembrane domains M3 and M4, and an extracellular C-terminal domain (Fig. 1B). All the phosphorylation sites on these receptors have been mapped to the major intracellular loop between M3 and M4 (Table 1). In contrast, glutamate receptors appear to have a very large extracellular N-terminal domain, one membrane hairpin loop, three transmembrane domains, a large extracellular loop between transmembrane domains M3 and M4, and an intracellular C-terminal domain (Fig. 1C). Most phosphorylation sites on glutamate receptors have been shown to be on the intracellular C-terminal domain, although some have been suggested to be on the putative extracellular loop between M3 and M4 (Table 1). A variety of extracellular factors and intracellular signal transduction cascades are involved in regulating phosphorylation of these ligand-gated ion channels (Fig. 2). Once again, the AChR at the neuromuscular junction is the most fully understood system. Phosphorylation of the AChR by PKA is stimulated synaptically by the neuropeptide CGRP and in an autocrine fashion by adenosine released from the muscle in response to acetylcholine. In addition, acetylcholine, via calcium influx through the AChR, appears to activate calcium-dependent kinases including PKC to stimulate serine phosphorylation of the receptor. Presently, agrin is the only extracellular factor known to stimulate phosphorylation of the AChR on tyrosine residues. For glutamate receptors, non-NMDA receptor phosphorylation by PKA is stimulated by dopamine, while NMDA receptor phosphorylation by PKA and PKC can be induced via the activation of beta-adrenergic receptors, and metabotropic glutamate or opioid receptors, respectively. In addition, Ca2+ influx through the NMDA receptor has been shown to activate PKC. CaMKII, and calcineurin, resulting in phosphorylation of AMPA receptors (by CaMKII) and inactivation of NMDA receptors (at least in part through calcineurin). In contrast to the AChR and glutamate receptors, no information is presently available regarding the identities of the extracellular factors and intracellular signal transduction cascades that regulate phosphorylation of the GABA(A) receptor. Surely, future studies will be aimed at further clarifying the molecular mechanisms by which the central receptors are regulated. The presently understood functional effects of ligand-gated ion channel phosphorylation are diverse. At the neuromuscular junction, a regulation of the AChR desensitization rate by both serine and tyrosine phosphorylation has been demonstrated. In addition, tyrosine p","PeriodicalId":76981,"journal":{"name":"Advances in second messenger and phosphoprotein research","volume":"33 ","pages":"49-78"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21089348","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 304

G protein gated potassium channels. G蛋白门控钾通道。

Advances in second messenger and phosphoprotein research Pub Date : 1999-01-01 DOI: 10.1016/s1040-7952(99)80010-x

J L Sui, K Chan, M N Langan, M Vivaudou, D E Logothetis

引用次数: 27

Type-specific regulation of mammalian adenylyl cyclases by G protein pathways. 哺乳动物腺苷酸环化酶通过G蛋白途径的类型特异性调控。

Advances in second messenger and phosphoprotein research Pub Date : 1998-01-01 DOI: 10.1016/s1040-7952(98)80006-2

R Taussig, G Zimmermann

引用次数: 53

Class III adenylyl cyclases: regulation and underlying mechanisms. III类腺苷酸环化酶:调控和潜在机制。

Advances in second messenger and phosphoprotein research Pub Date : 1998-01-01 DOI: 10.1016/s1040-7952(98)80009-8

W J Tang, S Yan, C L Drum

引用次数: 24

Mammalian adenylyl cyclases. 哺乳动物腺苷酸环化酶。

Advances in second messenger and phosphoprotein research Pub Date : 1998-01-01 DOI: 10.1016/s1040-7952(98)80003-7

M J Smit, R Iyengar

引用次数: 72

Molecular diversity of the adenylyl cyclases. 腺苷酸环化酶的分子多样性。

Advances in second messenger and phosphoprotein research Pub Date : 1998-01-01 DOI: 10.1016/s1040-7952(98)80005-0

J Krupinski, J J Cali

引用次数: 27

Genetic characterization of adenylyl cyclase function. 腺苷酸环化酶功能的遗传特征。

Advances in second messenger and phosphoprotein research Pub Date : 1998-01-01 DOI: 10.1016/s1040-7952(98)80008-6

M J Cann, L R Levin

引用次数: 8

Ca(2+)-sensitive adenylyl cyclases. Ca(2+)敏感腺苷酸环化酶。

Advances in second messenger and phosphoprotein research Pub Date : 1998-01-01

D M Cooper, J W Karpen, K A Fagan, N E Mons

引用次数: 0