Related Experiment Video
Updated: May 11, 2026

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
Published on: November 11, 2018
Rab GTPase regulation of membrane identity
1Department of Biochemistry, Stanford University School of Medicine, 279 Campus Drive B400, Stanford, CA 94305-5307, USA. pfeffer@stanford.edu
Abstract:
A fundamental question in cell biology is how cells determine membrane compartment identity and the directionality with which cargoes pass through the secretory and endocytic pathways. The discovery of so-called 'Rab cascades' provides a satisfying molecular mechanism that helps to resolve this paradox. One Rab GTPase has the ability to template the localization of the subsequent acting Rab GTPase along a given transport pathway. Thus, in addition to determining compartment identity and functionality, Rab GTPases are likely able to order the events of membrane trafficking. This review will highlight recent advances in our understanding of Rabs and Rab cascades.
Related Concept Videos
Rab Proteins
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
GTPases and their Regulation
Large G-proteins, also known...
GTPases and their Regulation
Large G-proteins, also known...
Small GTPases - Ras and Rho
Three regulatory proteins control their activity:
Rab Cascades
Activation and Inactivation of G Proteins

