Visual arrestin in Limulus is phosphorylated at multiple sites in the light and in the dark.

Abstract:

:Arrestins participate in the termination of phototransduction in both vertebrates and invertebrates. However, the visual arrestins of invertebrates and vertebrates differ significantly from one another in that the invertebrate visual arrestins become phosphorylated rapidly in response to light while those in the photoreceptors of vertebrates do not. In an effort to understand the functional relevance of arrestin phosphorylation, we examined this process in the photoreceptors of the horseshoe crab Limulus polyphemus. We report that Limulus visual arrestin can be phosphorylated at three sites near its C-terminus and show that arrestin molecules phosphorylated on one, two, and three sites are normally present in both light- and dark-adapted photoreceptors. Light adaptation increases the amount of arrestin phosphorylated at three sites.

journal_name

Vis Neurosci

journal_title

Visual neuroscience

authors

Battelle BA,Andrews AW,Kempler KE,Edwards SC,Smith WC

doi

10.1017/s0952523800175145

subject

Has Abstract

pub_date

2000-09-01 00:00:00

pages

813-22

issue

5

eissn

0952-5238

issn

1469-8714

pii

S0952523800175145

journal_volume

17

pub_type

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