bioRxivCell BiologyPreprint
Mechanistic dissection of BLTP2 targeting to ER-PM contact sites
Sarah D. NeumaniD, Amy T. Cavanagh, Nicole Sheffels, Elizabeth ConibeariD, Arash BashirullahiD
Abstract
The bridge-like lipid transfer proteins (BLTPs) are a novel superfamily of rod-shaped lipid transporters that engage in bulk non-vesicular movement of lipids at organelle membrane contact sites. The molecular and cellular functions of these proteins are still emerging; however, it is clear that one key aspect that regulates BLTP function is targeting to the appropriate membrane contact site(s). Here, we use Drosophila as a model system to dissect the mechanisms that drive targeting of BLTP2 (hobbit in Drosophila) to endoplasmic reticulum-plasma membrane (ER-PM) contact sites. We demonstrate that a conserved adapter protein, which we name bilbobaggins (bbo), is required for targeting of Hobbit to ER-PM contacts; importantly, loss of bbo phenocopies loss of hobbit, indicating that bbo is required for hobbit function. Additionally, our structure-function analyses show that cis-acting sequences in the C-terminal tail of Hobbit are also required for ER-PM targeting. Crucially, our data indicates that that these cis-acting sequences and Bbo binding are independent and likely sequential mechanisms that we propose function like a "hook" and "latch" to govern Hobbit targeting. Thus, we define a new regulatory paradigm governing targeting of BLTPs to membrane contact sites.
- Citations
- 0
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Hoi1 targets the yeast BLTP2 protein to ER-PM contact sites to regulate lipid homeostasis
Samantha Katarzyna Dziurdzik, Vaishnavi Sridhar, … Elizabeth Conibear·bioRxiv·Feb 11, 2025
- Multiple interactions mediate the localization of BLTP2 at ER-PM contacts to control plasma membrane dynamics
Anbang Dai, Peng Xu, … Pietro V. De Camilli·bioRxiv·Feb 7, 2025
- The Hob proteins are novel and conserved lipid binding proteins at ER-PM contact site
S. D. Neuman, J. R. Jorgensen, … A. Bashirullah·bioRxiv·Mar 2, 2021
- Bridge-like lipid transfer protein family member 2 suppresses ciliogenesis
J. Parolek, C. G. Burd·bioRxiv·Dec 7, 2023
- Structural basis of bulk lipid transfer by bridge-like lipid transfer protein LPD-3
Yunsik Kang, Katherine S. Lehmann, … Sarah Clark·NaturePeer-reviewed·Apr 23, 2025
- The molecular mechanism of lipid uptake by membrane-anchored bridge-like lipid transfer proteins.
Daniel Álvarez, Paige Chandran Blair, … Stefano Vanni·Proceedings of the National Academy of SciencesPeer-reviewed·Jan 21, 2026