Suppr超能文献

鲎眼中的钙/钙调蛋白依赖性蛋白激酶II与抑制蛋白磷酸化

Calcium/calmodulin-dependent protein kinase II and arrestin phosphorylation in Limulus eyes.

作者信息

Calman B G, Andrews A W, Rissler H M, Edwards S C, Battelle B A

机构信息

Whitney Laboratory, University of Florida, St. Augustine 32086, USA.

出版信息

J Photochem Photobiol B. 1996 Aug;35(1-2):33-44. doi: 10.1016/1011-1344(96)07312-5.

Abstract

In rhabdomeral photoreceptors, light stimulates the phosphorylation of arrestin, a protein critical for quenching the photoresponse, by activating a calcium/calmodulin-dependent protein kinase (CaM PK). Here we present biochemical evidence that a CaM PK that phosphorylates arrestin in Limulus eyes is structurally similar to mammalian CaM PK II. In addition, cDNAs encoding proteins homologous to mammalian and Drosophila CaM PK II in the catalytic and regulatory domains were cloned and sequenced from a Limulus lateral eye cDNA library. The Limulus sequences are unique, however, in that they lack most of the association domain. The proteins encoded by these sequences may phosphorylate arrestin.

摘要

在横纹肌光感受器中,光通过激活钙/钙调蛋白依赖性蛋白激酶(CaM PK)刺激抑制蛋白的磷酸化,抑制蛋白是终止光反应的关键蛋白。在此,我们提供生化证据表明,在鲎眼中使抑制蛋白磷酸化的CaM PK在结构上与哺乳动物的CaM PK II相似。此外,从鲎侧眼cDNA文库中克隆并测序了在催化和调节结构域与哺乳动物及果蝇CaM PK II同源的蛋白质的cDNA。然而,鲎的序列具有独特性,因为它们缺少大部分结合结构域。这些序列编码的蛋白质可能使抑制蛋白磷酸化。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验