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Updated: Aug 9, 2025

Imaging FITC-dextran as a Reporter for Regulated Exocytosis
Published on: June 20, 2018
Regulation of cargo exocytosis by a Reps1-Ralbp1-RalA module
Shifeng Wang1,2, Xu Chen1, Lauren Crisman1
1Department of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, CO 80309, USA.
Abstract:
Surface levels of membrane proteins are determined by a dynamic balance between exocytosis-mediated surface delivery and endocytosis-dependent retrieval from the cell surface. Imbalances in surface protein levels perturb surface protein homeostasis and cause major forms of human disease such as type 2 diabetes and neurological disorders. Here, we found a Reps1-Ralbp1-RalA module in the exocytic pathway broadly regulating surface protein levels. Reps1 and Ralbp1 form a binary complex that recognizes RalA, a vesicle-bound small guanosine triphosphatases (GTPase) promoting exocytosis through interacting with the exocyst complex. RalA binding results in Reps1 release and formation of a Ralbp1-RalA binary complex. Ralbp1 selectively recognizes GTP-bound RalA but is not a RalA effector. Instead, Ralbp1 binding maintains RalA in an active GTP-bound state. These studies uncovered a segment in the exocytic pathway and, more broadly, revealed a previously unrecognized regulatory mechanism for small GTPases, GTP state stabilization.
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