In:
Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 95, No. 10 ( 1998-05-12), p. 5584-5589
Abstract:
RGS4, a mammalian GTPase activating protein for G protein α
subunits, was identified by its ability to inhibit the pheromone response pathway in Saccharomyces cerevisiae . To define
regions of RGS4 necessary for its function in vivo , we
assayed mutants for activity in this system. Deletion of the N-terminal 33 aa of RGS4 (Δ1–33) yielded a nonfunctional protein and loss of
plasma membrane localization. These functions were restored by addition of a C-terminal membrane-targeting sequence to RGS4 (Δ1–33). Thus,
plasma membrane localization is tightly coupled with the ability of RGS4 to inhibit signaling. Fusion of the N-terminal 33 aa of RGS4 to
green fluorescent protein was sufficient to localize an otherwise soluble protein to the plasma membrane, defining this N-terminal region
as a plasma membrane anchorage domain. RGS4 is palmitoylated, with Cys-2 and Cys-12 the likely sites of palmitoylation. Surprisingly,
mutation of the cysteine residues within the N-terminal domain of RGS4 did not affect plasma membrane localization in yeast or the ability to
inhibit signaling. Features of the N-terminal domain other than palmitoylation are responsible for the plasma membrane association of
RGS4 and its ability to inhibit pheromone response in yeast.
Type of Medium:
Online Resource
ISSN:
0027-8424
,
1091-6490
DOI:
10.1073/pnas.95.10.5584
Language:
English
Publisher:
Proceedings of the National Academy of Sciences
Publication Date:
1998
detail.hit.zdb_id:
209104-5
detail.hit.zdb_id:
1461794-8
SSG:
11
SSG:
12
