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ER-PM contacts regulate apical domain formation in hepatocytes

Gary Hong Chun Chung, Jemima J. Burden, Maëlle Lorvellec, Paul Gissen, Christopher J. Stefan
doi: https://doi.org/10.1101/2020.04.23.057521
Gary Hong Chun Chung
1MRC Laboratory for Molecular Cell Biology, University College London, Gower Street, London WC1E 6BT, UK
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Jemima J. Burden
1MRC Laboratory for Molecular Cell Biology, University College London, Gower Street, London WC1E 6BT, UK
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  • For correspondence: j.burden@ucl.ac.uk c.stefan@ucl.ac.uk
Maëlle Lorvellec
1MRC Laboratory for Molecular Cell Biology, University College London, Gower Street, London WC1E 6BT, UK
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Paul Gissen
1MRC Laboratory for Molecular Cell Biology, University College London, Gower Street, London WC1E 6BT, UK
2NIHR Great Ormond Street Hospital Biomedical Research Centre, University College London, Ormond Street, London, WC1N 1EH, UK
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Christopher J. Stefan
1MRC Laboratory for Molecular Cell Biology, University College London, Gower Street, London WC1E 6BT, UK
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  • For correspondence: j.burden@ucl.ac.uk c.stefan@ucl.ac.uk
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Abstract

Apico-basal membrane polarity is fundamental for epithelial cell development and function. Polarity factors including the small GTPase Cdc42, the Par3/Par6/aPKC complex, and cytoskeletal proteins are recruited by the anionic lipids phosphatidylinositol 4,5-bisphosphate and phosphatidylserine. But how these lipids accumulate at polarised sites remains unclear. We have examined roles of contacts between the endoplasmic reticulum and plasma membrane (ER-PM contacts) in generating lipid gradients during apical domain formation. Comprehensive electron microscopy analyses in hepatocytes and epithelial spheroids revealed two distinct ER-PM contact architectures that are spatially linked to apical and baso-lateral domains. Moreover, apical domain formation was delayed in HepG2 cells upon modulating the ER-PM contact proteins E-Syt1 and ORP5. We propose ER-PM contacts regulate apico-basal polarity via the lipid transfer proteins E-Syt1 and ORP5. Importantly, our findings suggest that the spatial organisation of ER-PM contacts is a conserved feature of polarised epithelial cells.

Competing Interest Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted April 24, 2020.
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ER-PM contacts regulate apical domain formation in hepatocytes
Gary Hong Chun Chung, Jemima J. Burden, Maëlle Lorvellec, Paul Gissen, Christopher J. Stefan
bioRxiv 2020.04.23.057521; doi: https://doi.org/10.1101/2020.04.23.057521
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ER-PM contacts regulate apical domain formation in hepatocytes
Gary Hong Chun Chung, Jemima J. Burden, Maëlle Lorvellec, Paul Gissen, Christopher J. Stefan
bioRxiv 2020.04.23.057521; doi: https://doi.org/10.1101/2020.04.23.057521

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