Clathrin-coated vesicles bearing GAIP possess GTPase-activating protein activity in vitro (Q24653707)

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E Elenko

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J M McCaffery

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L DeVries

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M G Farquhar

Proceedings of the National Academy of Sciences of the United States of America

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language of work or name

English

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publication date

8 June 1999

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published in

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volume

96

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issue

12

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page(s)

6722-7

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cites work

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RGS-GAIP, a GTPase-activating protein for Galphai heterotrimeric G proteins, is located on clathrin-coated vesicles

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The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro

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GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits

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GAIP, a protein that specifically interacts with the trimeric G protein G alpha i3, is a member of a protein family with a highly conserved core domain

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A single mutation Asp229 --> Ser confers upon Gs alpha the ability to interact with regulators of G protein signaling

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