Arrestin from nucleated red blood cells binds to bovine rhodopsin in a light-dependent manner.

Abstract:

:Using a panel of monoclonal antibodies, it has previously been demonstrated that the cytosol of nucleated red cells (trout and turkey) contains a protein similar to arrestin, a soluble protein found so far only in the photosensitive cells and which, by binding to photoexcited rhodopsin, inhibits the phototransduction process. The role of this arrestin-like protein in non-photosensitive cells is questionable. In this report we present evidence that partially purified red blood cell arrestin (RBC arrestin) behaves functionally like bovine retinal arrestin: it binds to phosphorylated bovine rhodopsin only when this receptor has been photoactivated. Thus RBC arrestin and bovine retinal arrestin are closely related both structurally and functionally. By analogy with the function of retinal arrestin, it is proposed that RBC arrestin is involved in desensitization of membrane transport proteins and/or adrenergic receptors.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Scheuring U,Franco M,Fievet B,Guizouarn H,Mirshahi M,Faure JP,Motais R

doi

10.1016/0014-5793(90)80540-y

subject

Has Abstract

pub_date

1990-12-10 00:00:00

pages

192-6

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(90)80540-Y

journal_volume

276

pub_type

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