| Literature DB >> 8823933 |
B G Calman1, A W Andrews, H M Rissler, S C Edwards, B A Battelle.
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.Entities:
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Year: 1996 PMID: 8823933 DOI: 10.1016/1011-1344(96)07312-5
Source DB: PubMed Journal: J Photochem Photobiol B ISSN: 1011-1344 Impact factor: 6.252