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Survey of nucleotide-specific Rab GTPase interactions reveals multiple Rab effectors
Preprint   Open access

Survey of nucleotide-specific Rab GTPase interactions reveals multiple Rab effectors

Tabitha A Peterson, Christopher P Ptak and Robert C Piper
bioRxiv
Cold Spring Harbor Laboratory
09/17/2026
DOI: 10.64898/2026.09.15.751902
PMCID: PMC13596360
PMID: 42779768
url
https://doi.org/10.64898/2026.09.15.751902View
Preprint (Author's original) This preprint has not been evaluated by subject experts through peer review. Preprints may undergo extensive changes and/or become peer-reviewed journal articles. Open Access

Abstract

Rab GTPases control myriad molecular functions by acting as a nucleotide-dependent switch for protein-protein interactions localized in discrete subcellular regions. Finding additional molecular roles for Rab GTPases depends on expanding the identification of their nucleotide-dependent interactions. Here we compare the interactome of Rab GTPases using a comprehensive large-scale yeast 2-hybrid approach powered by quantitative high-throughput sequencing, which was used to find interactions of the major mammalian Rab isoforms locked in a GDP or GTP conformation. These data showed an expanded set of interactions specific for GTP-bound Rab proteins, which many know Rab effectors shown capable of binding a wider repertoire of partners than previously appreciated. We also identified the RGS domain of Snx13 and Snx14 as a new Rab GTPase-binding domain that may bridge these ER-localized proteins with Rab5 and Rab11 endosomal compartments, respectively.

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