Abstract
Regulator of G protein signaling (RGS) proteins are GTPase-activating proteins (GAP) for G protein α-subunits and are thought to be responsible for rapid deactivation of G protein mediated signaling pathway. In this present study, we demonstrate that PA is the most efficient candidate to inhibit GAP activity of RGS4. The functional significance of N-terminus of RGS4 in respose to PA-granted inhibition on GAP activity has been studied with the site mutation in the N-terminus of RGS4. These site-directed mutations in the N-terminal domain do not severely disrupt its association with liposomes of PA. However, RGS4L23E diminishes the inhibition of GAP activity by PA compared with the wild type RGS4, whereas RGSR22E abrogates the inhibitory effect by PA on GAP activity. The correspondent conformational discrepancy in the RGS domain of these mutants in the presence of PA vesicles was detected from fluorescence experiments. It is suggested that the functional pertinence between the N-terminus and RGS domain may be important to modulate PA-conferred inhibitory effect on its GAP activity.
| Original language | English |
|---|---|
| Pages (from-to) | 213-224 |
| Number of pages | 12 |
| Journal | Bioscience Reports |
| Volume | 23 |
| Issue number | 4 |
| DOIs | |
| State | Published - Aug 2003 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
Cite this
The Mutation in the N-terminal Domain of RGS4 Disrupts PA-conferred Inhibitory Effect on GAP Activity. / Ou-Yang, Ying Shi; Tu, Yaping; Yang, Fuyu.
In: Bioscience Reports, Vol. 23, No. 4, 08.2003, p. 213-224.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The Mutation in the N-terminal Domain of RGS4 Disrupts PA-conferred Inhibitory Effect on GAP Activity
AU - Ou-Yang, Ying Shi
AU - Tu, Yaping
AU - Yang, Fuyu
PY - 2003/8
Y1 - 2003/8
N2 - Regulator of G protein signaling (RGS) proteins are GTPase-activating proteins (GAP) for G protein α-subunits and are thought to be responsible for rapid deactivation of G protein mediated signaling pathway. In this present study, we demonstrate that PA is the most efficient candidate to inhibit GAP activity of RGS4. The functional significance of N-terminus of RGS4 in respose to PA-granted inhibition on GAP activity has been studied with the site mutation in the N-terminus of RGS4. These site-directed mutations in the N-terminal domain do not severely disrupt its association with liposomes of PA. However, RGS4L23E diminishes the inhibition of GAP activity by PA compared with the wild type RGS4, whereas RGSR22E abrogates the inhibitory effect by PA on GAP activity. The correspondent conformational discrepancy in the RGS domain of these mutants in the presence of PA vesicles was detected from fluorescence experiments. It is suggested that the functional pertinence between the N-terminus and RGS domain may be important to modulate PA-conferred inhibitory effect on its GAP activity.
AB - Regulator of G protein signaling (RGS) proteins are GTPase-activating proteins (GAP) for G protein α-subunits and are thought to be responsible for rapid deactivation of G protein mediated signaling pathway. In this present study, we demonstrate that PA is the most efficient candidate to inhibit GAP activity of RGS4. The functional significance of N-terminus of RGS4 in respose to PA-granted inhibition on GAP activity has been studied with the site mutation in the N-terminus of RGS4. These site-directed mutations in the N-terminal domain do not severely disrupt its association with liposomes of PA. However, RGS4L23E diminishes the inhibition of GAP activity by PA compared with the wild type RGS4, whereas RGSR22E abrogates the inhibitory effect by PA on GAP activity. The correspondent conformational discrepancy in the RGS domain of these mutants in the presence of PA vesicles was detected from fluorescence experiments. It is suggested that the functional pertinence between the N-terminus and RGS domain may be important to modulate PA-conferred inhibitory effect on its GAP activity.
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UR - http://www.scopus.com/inward/citedby.url?scp=0346501884&partnerID=8YFLogxK
U2 - 10.1023/B:BIRE.0000007694.71158.02
DO - 10.1023/B:BIRE.0000007694.71158.02
M3 - Article
VL - 23
SP - 213
EP - 224
JO - Bioscience Reports
JF - Bioscience Reports
SN - 0144-8463
IS - 4
ER -