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Peer-reviewedCC BYFEBS Letters

Peripheral lysosomes recruit PLEKHG3 to focal adhesions and restrain protrusion dynamics

  • Rainer Ettelt1,2,3
  • Ana-Maria Șandru1,2,3
  • Georg Vucak1,2,3
  • Sebastian Didusch1,2,3
  • Biljana Riemelmoser4,5
  • Karin Ehrenreiter1
  • Markus Hartl6,2
  • Lukas Alfons Huber7
  • Manuela Baccarini1,2
7 affiliations
  1. 1Max Perutz Labs Vienna Austria
  2. 2University of Vienna Vienna Austria
  3. 3Vienna BioCenter PhD Program Doctoral School of the University of Vienna and Medical University of Vienna Vienna Austria
  4. 4Department of Medicine, Faculty of Medicine University of Geneva Geneva Switzerland
  5. 5Department of Pathology and Immunology, Faculty of Medicine University of Geneva Geneva Switzerland
  6. 6Max Perutz Labs Mass Spectrometry Facility Vienna Austria
  7. 7Medizinische Universität Innsbruck Biocenter Institute of Cell Biology Innsbruck Austria
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Abstract

Lysosomes are dynamic organelles regulating metabolic signaling by recruiting cytosolic molecules to protein platforms on their limiting membrane. We used proximity labeling to define interactors and vicinal proteins of LAMTOR3, a component of the Ragulator scaffold that controls mTORC1 signaling and lysosome positioning. The screen has yielded several previously unappreciated interactors, including an actin remodeling network. Here, we characterize the RhoGEF PLEKHG3 as a LAMTOR3 vicinal protein colocalizing with peripheral lysosomes and cortical F-actin at focal adhesion sites. Forced peripheral dispersion of lysosomes drives PLEKHG3 accumulation at focal adhesions and decreases protrusive activity in both wild-type and PLEKHG3-deficient cells. Thus, lysosome positioning governs both PLEKHG3 localization and protrusive activity, yet the protrusion changes can occur independently of PLEKHG3.

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Cite

BibTeXRIS
BibTeX
@article{ettelt2026peripheral,
  title = {{Peripheral lysosomes recruit PLEKHG3 to focal adhesions and restrain protrusion dynamics}},
  author = {Rainer Ettelt and Ana-Maria Șandru and Georg Vucak and Sebastian Didusch and Biljana Riemelmoser and Karin Ehrenreiter and Markus Hartl and Lukas Alfons Huber and Manuela Baccarini},
  journal = {FEBS Letters},
  year = {2026},
  month = aug,
  doi = {10.1002/1873-3468.70428},
  url = {https://doi.org/10.1002/1873-3468.70428},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Peripheral lysosomes recruit PLEKHG3 to focal adhesions and restrain protrusion dynamics
AU  - Rainer Ettelt
AU  - Ana-Maria Șandru
AU  - Georg Vucak
AU  - Sebastian Didusch
AU  - Biljana Riemelmoser
AU  - Karin Ehrenreiter
AU  - Markus Hartl
AU  - Lukas Alfons Huber
AU  - Manuela Baccarini
PY  - 2026
DA  - 2026/08/10
JO  - FEBS Letters
DO  - 10.1002/1873-3468.70428
UR  - https://doi.org/10.1002/1873-3468.70428
AB  - Lysosomes are dynamic organelles regulating metabolic signaling by recruiting cytosolic molecules to protein platforms on their limiting membrane. We used proximity labeling to define interactors and vicinal proteins of LAMTOR3, a component of the Ragulator scaffold that controls mTORC1 signaling and lysosome positioning. The screen has yielded several previously unappreciated interactors, including an actin remodeling network. Here, we characterize the RhoGEF PLEKHG3 as a LAMTOR3 vicinal protein colocalizing with peripheral lysosomes and cortical F-actin at focal adhesion sites. Forced peripheral dispersion of lysosomes drives PLEKHG3 accumulation at focal adhesions and decreases protrusive activity in both wild-type and PLEKHG3-deficient cells. Thus, lysosome positioning governs both PLEKHG3 localization and protrusive activity, yet the protrusion changes can occur independently of PLEKHG3.
SN  - 0014-5793
SN  - 1873-3468
ER  -