Tricalbin proteins regulate plasma membrane phospholipid homeostasis
The evolutionarily conserved extended synaptotagmin (E-Syt) proteins are calcium-activated lipid transfer proteins that function at contacts between the ER and plasma membrane (ER-PM contacts). However, roles of the E-Syt family members in PM lipid organisation remain incomplete. Among the E-Syt fam...
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Published in | Life science alliance Vol. 5; no. 8; p. e202201430 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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Life Science Alliance LLC
01.08.2022
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Abstract | The evolutionarily conserved extended synaptotagmin (E-Syt) proteins are calcium-activated lipid transfer proteins that function at contacts between the ER and plasma membrane (ER-PM contacts). However, roles of the E-Syt family members in PM lipid organisation remain incomplete. Among the E-Syt family, the yeast tricalbin (Tcb) proteins are essential for PM integrity upon heat stress, but it is not known how they contribute to PM maintenance. Using quantitative lipidomics and microscopy, we find that the Tcb proteins regulate phosphatidylserine homeostasis at the PM. Moreover, upon heat-induced membrane stress, Tcb3 co-localises with the PM protein Sfk1 that is implicated in PM phospholipid asymmetry and integrity. The Tcb proteins also control the PM targeting of the known phosphatidylserine effector Pkc1 upon heat-induced stress. Phosphatidylserine has evolutionarily conserved roles in PM organisation, integrity, and repair. We propose that phospholipid regulation is an ancient essential function of E-Syt family members required for PM integrity. |
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AbstractList | The evolutionarily conserved extended synaptotagmin (E-Syt) proteins are calcium-activated lipid transfer proteins that function at contacts between the ER and plasma membrane (ER-PM contacts). However, roles of the E-Syt family members in PM lipid organisation remain incomplete. Among the E-Syt family, the yeast tricalbin (Tcb) proteins are essential for PM integrity upon heat stress, but it is not known how they contribute to PM maintenance. Using quantitative lipidomics and microscopy, we find that the Tcb proteins regulate phosphatidylserine homeostasis at the PM. Moreover, upon heat-induced membrane stress, Tcb3 co-localises with the PM protein Sfk1 that is implicated in PM phospholipid asymmetry and integrity. The Tcb proteins also control the PM targeting of the known phosphatidylserine effector Pkc1 upon heat-induced stress. Phosphatidylserine has evolutionarily conserved roles in PM organisation, integrity, and repair. We propose that phospholipid regulation is an ancient essential function of E-Syt family members required for PM integrity. The extended synaptotagmin (E-Syt) family are conserved proteins that function at membrane contacts. This study reveals that yeast E-Syt family members regulate phospholipid homeostasis necessary for plasma membrane integrity. The evolutionarily conserved extended synaptotagmin (E-Syt) proteins are calcium-activated lipid transfer proteins that function at contacts between the ER and plasma membrane (ER-PM contacts). However, roles of the E-Syt family members in PM lipid organisation remain incomplete. Among the E-Syt family, the yeast tricalbin (Tcb) proteins are essential for PM integrity upon heat stress, but it is not known how they contribute to PM maintenance. Using quantitative lipidomics and microscopy, we find that the Tcb proteins regulate phosphatidylserine homeostasis at the PM. Moreover, upon heat-induced membrane stress, Tcb3 co-localises with the PM protein Sfk1 that is implicated in PM phospholipid asymmetry and integrity. The Tcb proteins also control the PM targeting of the known phosphatidylserine effector Pkc1 upon heat-induced stress. Phosphatidylserine has evolutionarily conserved roles in PM organisation, integrity, and repair. We propose that phospholipid regulation is an ancient essential function of E-Syt family members required for PM integrity. |
Author | Stefan, Christopher J Chung, Gary Hc Thomas, Ffion B Bader, Jakob M Omnus, Deike J Kono, Nozomu |
AuthorAffiliation | 2 Department of Health Chemistry, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan 1 Medical Research Council Laboratory for Molecular Cell Biology, University College London, London, UK |
AuthorAffiliation_xml | – name: 1 Medical Research Council Laboratory for Molecular Cell Biology, University College London, London, UK – name: 2 Department of Health Chemistry, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan |
Author_xml | – sequence: 1 givenname: Ffion B surname: Thomas fullname: Thomas, Ffion B organization: Medical Research Council Laboratory for Molecular Cell Biology, University College London, London, UK – sequence: 2 givenname: Deike J surname: Omnus fullname: Omnus, Deike J organization: Medical Research Council Laboratory for Molecular Cell Biology, University College London, London, UK – sequence: 3 givenname: Jakob M orcidid: 0000-0002-6575-0609 surname: Bader fullname: Bader, Jakob M organization: Medical Research Council Laboratory for Molecular Cell Biology, University College London, London, UK – sequence: 4 givenname: Gary Hc orcidid: 0000-0001-6764-3041 surname: Chung fullname: Chung, Gary Hc organization: Medical Research Council Laboratory for Molecular Cell Biology, University College London, London, UK – sequence: 5 givenname: Nozomu orcidid: 0000-0002-0871-8477 surname: Kono fullname: Kono, Nozomu organization: Department of Health Chemistry, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan – sequence: 6 givenname: Christopher J orcidid: 0000-0002-4118-5721 surname: Stefan fullname: Stefan, Christopher J email: c.stefan@ucl.ac.uk organization: Medical Research Council Laboratory for Molecular Cell Biology, University College London, London, UK c.stefan@ucl.ac.uk |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/35440494$$D View this record in MEDLINE/PubMed |
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CitedBy_id | crossref_primary_10_1080_21505594_2023_2299183 crossref_primary_10_1073_pnas_2321991121 crossref_primary_10_1016_j_biochi_2023_09_003 crossref_primary_10_1016_j_ejcb_2023_151335 crossref_primary_10_1083_jcb_202308144 crossref_primary_10_3389_fpls_2024_1363555 crossref_primary_10_7554_eLife_74602 crossref_primary_10_1002_yea_3933 crossref_primary_10_1091_mbc_E23_01_0029 crossref_primary_10_1007_s00441_024_03858_x crossref_primary_10_1016_j_ceb_2023_102192 |
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Notes | Jakob M Bader’s present address is Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany. Deike J Omnus’s present address is Science for Life Laboratory, Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Stockholm, Sweden. |
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Snippet | The evolutionarily conserved extended synaptotagmin (E-Syt) proteins are calcium-activated lipid transfer proteins that function at contacts between the ER and... The extended synaptotagmin (E-Syt) family are conserved proteins that function at membrane contacts. This study reveals that yeast E-Syt family members... |
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SubjectTerms | Cell Membrane - metabolism Homeostasis Membrane Proteins - genetics Membrane Proteins - metabolism Phosphatidylserines - metabolism Phospholipids - metabolism Synaptotagmins - metabolism |
Title | Tricalbin proteins regulate plasma membrane phospholipid homeostasis |
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