Calman B G, Andrews A W, Rissler H M, Edwards S C, Battelle B A
Whitney Laboratory, University of Florida, St. Augustine 32086, USA.
J Photochem Photobiol B. 1996 Aug;35(1-2):33-44. doi: 10.1016/1011-1344(96)07312-5.
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.
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。