FEBS Letters | |
UV‐light‐dependent binding of a visual arrestin 1 isoform to photoreceptor membranes in a neuropteran (Ascalaphus) compound eye | |
Gerdon, Gabriele2  Draslar, Kazimir1  Schillo, Markus2  Paulsen, Reinhard2  Bentrop, Joachim2  | |
[1] Department of Biology, Biotechnical Faculty, University of Ljubljana, Vecna pot 111, SL-1000 Ljubljana, Slovenia;Lehrstuhl für Zell- und Neurobiologie, Zoologisches Institut, Universität Karlsruhe, Haid-und-Neustr. 9, D-76131 Karlsruhe, Germany | |
关键词: Arrestin; UV-absorbing rhodopsin; Light-dependent arrestin binding; Vision; Sensory cell; Am; Ascalaphus macaronius; Arr1; arrestin 1; Arr2; arrestin 2; Cv; Calliphora vicina; Dm; Drosophila melanogaster; GPCR; G-protein-coupled receptor; Hv; Heliothis virescens; M; metarhodopsin; P; rhodopsin; | |
DOI : 10.1016/S0014-5793(01)02287-6 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Arrestins are regulators of the active state of G-protein-coupled receptors. Towards elucidating the function of different arrestin subfamilies in sensory cells, we have isolated a novel arrestin 1, Am Arr1, from the UV photoreceptors of the neuropteran Ascalaphus macaronius. Am Arr1 forms a phylogenetic clade with antennal and visual Arr1 isoforms of invertebrates. Am Arr1 undergoes a light-dependent binding cycle to photoreceptor membranes, as reported earlier only for members of the arrestin 2 subfamily. This suggests a common control mechanism for the active state of invertebrate rhodopsins and G-protein-coupled receptors of antennal sensory cells. Furthermore, it implies that a strict correlation of distinct arrestin isoforms to distinct functions is not a general principle for invertebrate sensory cells.
【 授权许可】
Unknown
【 预 览 】
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