Survey of nucleotide-specific Rab GTPase interactions reveals multiple Rab effectors
- 1University of Iowa
Abstract
Rab GTPases control myriad molecular functions by acting as a nucleotide-dependent switch for protein-protein interactions localized in discrete subcellular regions (Zerial and McBride, 2001). 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 revealed an expanded set of interactions specific for GTP-bound Rab proteins, with many known Rab effectors capable of binding a wider repertoire of Rab 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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BibTeX
@misc{peterson2026survey,
title = {{Survey of nucleotide-specific Rab GTPase interactions reveals multiple Rab effectors}},
author = {T. A. Peterson and C. Ptak and R. C. Piper},
howpublished = {bioRxiv},
year = {2026},
month = sep,
doi = {10.64898/2026.09.15.751902},
url = {https://www.biorxiv.org/content/10.64898/2026.09.15.751902v1},
note = {CC BY},
}
RIS
TY - UNPB
TI - Survey of nucleotide-specific Rab GTPase interactions reveals multiple Rab effectors
AU - T. A. Peterson
AU - C. Ptak
AU - R. C. Piper
PY - 2026
DA - 2026/09/15
PB - bioRxiv
DO - 10.64898/2026.09.15.751902
UR - https://www.biorxiv.org/content/10.64898/2026.09.15.751902v1
AB - Rab GTPases control myriad molecular functions by acting as a nucleotide-dependent switch for protein-protein interactions localized in discrete subcellular regions (Zerial and McBride, 2001). 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 revealed an expanded set of interactions specific for GTP-bound Rab proteins, with many known Rab effectors capable of binding a wider repertoire of Rab 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.
ER -