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Article

The KDEL receptor regulates a GTPase-activating protein for ADP-ribosylation factor 1 by interacting with its non-catalytic domain.

The Journal of biological chemistry - 16 Jul 1999

Aoe T, Huber I, Vasudevan C, Watkins S C, Romero G, Cassel D, Hsu V W

Abstract excerpt

ADP-ribosylation factor 1 (ARF1) is a key regulator of transport in the secretory system. Like all small GTPases, deactivation of ARF1 requires a GTPase-activating protein (GAP) that promotes hydrolysis of GTP to GDP on ARF1. Structure-function analysis of a GAP for ARF1 revealed that its activity in vivo requires not only a domain that catalyzes hydrolysis of GTP on ARF1 but also a non-catalytic domain. In this...

Topics

ADP-Ribosylation Factor 1
ADP-Ribosylation Factors
Animals
COS Cells
Catalytic Domain
GTP-Binding Proteins
GTPase-Activating Proteins
HeLa Cells
Humans
Kinetics
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Binding

Proteins

Receptors, Peptide

Source

Identifiers

PMID: 10400684
DOI: 10.1074/jbc.274.29.20545

Genes

ARF1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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The KDEL receptor regulates a GTPase-activating protein for ADP-ribosylation factor 1 by interacting with its non-catalytic domain.PMID 10400684Read ↗

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