The Ral small GTPase is an essential regulator of exocyst complex function in secretion.

Authors

You Wu, David J Reiner

Published in

The Journal of cell biology. Volume 225. Issue 11. Nov 02, 2026. Epub Oct 06, 2026.

Abstract

Ral GTPases have long been proposed as regulators of the metazoan exocyst, a conserved secretory vesicle-tethering complex, but direct evidence for this role has been scarce. In contrast, the well-studied yeast exocyst relies on multiple Rab GTPases to regulate function, but yeast do not encode Ral. Using Caenorhabditis elegans, we demonstrate that endogenous RAL-1 directly engages the exocyst through conserved binding sites in its subunits. Loss of RAL-1 disrupts dendritic arborization of PVD sensory neurons, impairs vesicle trafficking, and causes broad developmental defects, acting both cell autonomously in neurons and non-autonomously through supporting epithelial cells. Structure-guided genome editing of RAL-1-exocyst interfaces produced synthetic phenotypes, underscoring the physiological importance of these contacts. Taken together, our findings establish RAL-1 as a bona fide regulator of the metazoan exocyst in vivo and suggest that Ral-exocyst interactions operate in parallel with other secretory pathways. More broadly, this work positions C. elegans as a powerful system to dissect Ral-exocyst mechanisms across molecular, cellular, and developmental scales.

PMID:
42836793
Bibliographic data and abstract were imported from PubMed on 06 Oct 2026.

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