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J. Biol. Chem., Vol. 268, Issue 21, 15640-15648, Jul, 1993
R Sterne-Marr, VV Gurevich, P Goldsmith, RC Bodine, C Sanders, LA Donoso and JL Benovic
Retinal arrestin (S-antigen) inactivates the phototransduction cascade by
binding to light-activated phosphorylated rhodopsin and thereby "arresting"
coupling to the G protein transducin. beta-Arrestin (beta arr), a
ubiquitous arrestin homolog, acts analogously to desensitize the beta
2-adrenergic receptor by disrupting Gs receptor interaction. In an attempt
to identify additional "arrestins" which might regulate the multitude of G
protein-coupled receptors, we have isolated two bovine brain cDNAs which
encode polypeptide variants of an arrestin homolog which we have designated
arrestin3 (arr3). The open reading frames of these two cDNAs are identical
except that the long form, arr3L, contains an 11-amino-acid insert between
residues 361 and 362. Arr3 is more closely related to bovine beta arr (78%
identity) than to bovine visual arrestin (56% identity). Polymerase chain
reaction amplification of RNA and immunoblotting of lysates with an arr3-
specific antibody suggest that the short form, arr3S, is the major form of
arr3 in all bovine tissues and that it is most abundant in the spleen.
Furthermore, polymerase chain reaction amplification of beta arr mRNA
indicates that in several tissues (lung, liver, spleen, and pituitary), the
major form of beta arr lacks 8 amino acids which are present in brain beta
arr. Immunoblotting with an antibody which recognizes beta arr and arr3
with equal sensitivity demonstrates that beta arr (either the long or the
short polypeptide) is the major arrestin in all (non-photoreceptor bearing)
tissues examined. These observations suggest that in some tissues, as many
as four arrestin homolog variants may play a role in the regulation of G
protein-coupled receptors.
Polypeptide variants of beta-arrestin and arrestin3
Department of Pharmacology, Jefferson Cancer Institute, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
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