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Related Experiment Video

Updated: Jun 5, 2026

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analysis and Imaging

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Published on: October 3, 2017

Rab27a, actin and beta-cell endocytosis.

Toshihide Kimura¹, Ichiro Niki

¹Department of Pharmacology, Oita University Faculty of Medicine, 1-1 Idaigaoka, Hasama, Yufu, Oita, Japan.

Endocrine Journal

|December 29, 2010

Summary

The small GTPase Rab27a regulates insulin granule release. Its interaction with coronin 3 controls post-exocytotic stages, crucial for membrane recycling in pancreatic beta-cells.

Area of Science:

Endocrinology
Cell Biology
Molecular Biology

Background:

Insulin release from pancreatic beta-cells is tightly regulated.
The small GTPase Rab27a influences pre-exocytotic stages, affecting insulin granule pool size.

Purpose of the Study:

To investigate the role of Rab27a and its interacting proteins in insulin secretion.
To elucidate the function of coronin 3 in the context of Rab27a signaling.

Main Methods:

Screening for Rab27a-interacting proteins.
Characterization of the Rab27a-coronin 3 interaction and its functional consequences.

Main Results:

Coronin 3 was identified as a Rab27a-interacting protein.
Coronin 3 binds GDP-Rab27a and regulates post-exocytotic stages by reorganizing the actin cytoskeleton.

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This interaction is glucose-dependent, suggesting a role in stimulus-endocytosis coupling.

Conclusions:

Rab27a plays a dual role in insulin secretion, regulating both pre- and post-exocytotic stages.
The GDP-bound form of Rab27a, interacting with coronin 3, is key for membrane recycling of insulin granules.
Rab27a is a critical molecule linking cellular stimulation to endocytosis in pancreatic beta-cells.