Journal
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 81
Volume 81, Issue -, Pages 637-659Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-052810-093700
Keywords
Rab; ARF; guanine nucleotide exchange factor; GTPase-activating protein; effector; vesicular transport
Categories
Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM035370, R01GM082861, R37GM035370] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R37 GM035370, GM082861, R01 GM035370, R01 GM082861, GM35370] Funding Source: Medline
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Members of the Rab or ARF/Sar branches of the Ras GTPase superfamily regulate almost every step of intracellular membrane traffic. A rapidly growing body of evidence indicates that these GTPases do not act as lone agents but are networked to one another through a variety of mechanisms to coordinate the individual events of one stage of transport and to link together the different stages of an entire transport pathway. These mechanisms include guanine nucleotide exchange factor (GEF) cascades, GTPase-activating protein (GAP) cascades, effectors that bind to multiple GTPases, and positive-feedback loops generated by exchange factor-effector interactions. Together these mechanisms can lead to an ordered series of transitions from one GTPase to the next. As each GTPase recruits a unique set of effectors, these transitions help to define changes in the functionality of the membrane compartments with which they are associated.
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