Abstract:
:Regulator of G protein signaling (RGS) proteins are GTPase-activating proteins (GAP) for G protein alpha-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.
journal_name
Biosci Repjournal_title
Bioscience reportsauthors
Ou-Yang YS,Tu Y,Yang Fdoi
10.1023/b:bire.0000007694.71158.02keywords:
subject
Has Abstractpub_date
2003-08-01 00:00:00pages
213-24issue
4eissn
0144-8463issn
1573-4935journal_volume
23pub_type
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journal_title:Bioscience reports
pub_type: 杂志文章,评审
doi:10.1007/BF01122123
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journal_title:Bioscience reports
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journal_title:Bioscience reports
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journal_title:Bioscience reports
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journal_title:Bioscience reports
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更新日期:2011-04-01 00:00:00
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journal_title:Bioscience reports
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doi:10.1007/BF01122227
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journal_title:Bioscience reports
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journal_title:Bioscience reports
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journal_title:Bioscience reports
pub_type: 杂志文章,评审
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journal_title:Bioscience reports
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更新日期:2015-10-12 00:00:00
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journal_title:Bioscience reports
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更新日期:1984-03-01 00:00:00
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journal_title:Bioscience reports
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journal_title:Bioscience reports
pub_type: 杂志文章
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