@inbook{b40056d07bca4d08a7852f60d7ac79be,
title = "Purification and In Vitro functional analyses of RGS12 and RGS14 GoLoco motif peptides",
abstract = "The GoLoco motif is a short polypeptide sequence that binds to heterotrimeric G-protein α subunits of the adenylyl cyclase-inhibitory (Gαio) subclass in a nucleotide-dependent manner (i.e., solely to the GDP-bound ground state). This article describes methods used for the expression, purification, and in vitro evaluation of membrane-permeant tag fusion peptides derived from the GoLoco motif regions of {"}regulator of G-protein signaling{"} proteins type 12 (RGS12) and 14 (RGS14) and a consensus GoLoco sequence from the multiple GoLoco motif protein AGS3. Three different fluorescence-based assays are described for evaluating the in vitro function of these GoLoco peptides as guanine nucleotide dissociation inhibitors, including measurements of GTPγS binding and Gα subunit activation by the planar ion aluminum tetrafluoride.",
author = "Kimple, {Randall J.} and Willard, {Francis S.} and Siderovski, {David P.}",
year = "2004",
month = jan,
day = "1",
doi = "10.1016/S0076-6879(04)90026-2",
language = "English",
series = "Methods in Enzymology",
publisher = "Academic Press Inc.",
pages = "419--436",
booktitle = "Regulators of G-Protein Signaling, Part B",
}