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Recoverin inhibits the phosphorylation of dark-adapted rhodopsin more than it does that of bleached rhodopsin: A possible mechanism through which rhodopsin kinase is prevented from participation in a side reactionстатья
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Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Senin I.I., Dean K.R., Zargarov A.A., Akhtar M., Philippov P.P.
- Журнал: Biochemical Journal
- Том: 321
- Год издания: 1997
- Издательство: Portland Press, Ltd.
- Местоположение издательства: United Kingdom
- Первая страница: 551
- Последняя страница: 555
- Аннотация: In its resting state rhodopsin kinase is present in an inactive form and is activated after interaction with light-activated rhodopsin (Rho*). The activated rhodopsin kinase then phosphorylates Rho* but is also able to catalyse the phosphorylation of dark-adapted rhodopsin. A consequence of the latter behaviour of the activated kinase is that at low levels of bleach a large number of phosphoryl groups are incorporated per mol of Rho*. Recoverin- and Ca2+-dependent inhibition of rhodopsin kinase was found to be inversely related to the extent of bleaching; the lower the fraction of rhodopsin bleached, the greater the inhibition. The IC50 of recoverin is approx. 1 mu M at a 0.2 % level of bleach and about 5 mu M in a fully bleached sample. The inhibitory effect of recoverin was studied separately on the phosphorylation of rhodopsin and Rho*. The formation of phosphorylated rhodopsin was inhibited 4.5-fold more strongly than that of phosphorylated Rho*. These results are interpreted to suggest that one of the roles of the recoverin-dependent regulation of the activity of rhodopsin kinase is to prevent the enzyme from participating in the unwanted phosphorylation of dark-adapted rhodopsin, directing it to fulfil its ’correct’ function of quenching the transduction activity of Rho*.
- Добавил в систему: Филиппов Павел Павлович