Biochemical characterization of Rab3-GTPase-activating protein reveals a mechanism similar to that of Ras-GAP (Q22254280)

RAB3A, member RAS oncogene family

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regulation of GTPase activity

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Uncharacterized protein Dmel_CG31935

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Rab3 GTPase-activating protein catalytic subunit CELE_F20D1.6

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A Clabecq

1

A

Clabecq

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PubMed

8 February 2023

J P Henry

series ordinal

2

author given names

J P

author last names

Henry

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PubMed

8 February 2023

F Darchen

series ordinal

3

author given names

F

author last names

Darchen

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PubMed

Journal of Biological Chemistry

8 February 2023

language of work or name

English

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publication date

13 October 2000

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published in

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volume

275

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issue

41

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page(s)

31786-91

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cites work

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The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion

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A yeast GTPase-activating protein that interacts specifically with a member of the Ypt/Rab family

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GTPase-activating proteins: helping hands to complement an active site

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Structural basis of activation and GTP hydrolysis in Rab proteins

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Ras binding to a C-terminal region of GAP

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Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis

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Transient Kinetic Studies on the Interaction of Ras and the Ras-Binding Domain of c-Raf-1 Reveal Rapid Equilibration of the Complex†

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Ca2 /calmodulin causes Rab3A to dissociate from synaptic membranes

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Activation of ADP-ribosylation factor 1 GTPase-activating protein by phosphatidylcholine-derived diacylglycerols

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Formation of a Transition-State Analog of the Ras GTPase Reaction by Ras GDP, Tetrafluoroaluminate, and GTPase-Activating Proteins

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7 January 2021

Identifiers

DOI

10.1074/JBC.M003705200

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