Publications

We investigate how lipid flux and membrane architecture are organized, bridging advanced cell biological and in-cell structural approaches across scales.

Highlighted papers

• Salo V.T.*, Klug Y.A.*, Sapia J.*, Deme J.C., Tocci J.M., Babenko A., Jacob R.S., Eikmeier N., Zagoriy E., Goetz S.K., Campomanes P., Banterle N., Lea S.M., Vanni S., Carvalho P., Mahamid J.
  Regulated conformational transitions in seipin define a functional ER–lipid droplet interface.
  bioRxiv (2026).
  10.64898/2026.06.22.733769
  Combined in-cell cryo-ET, structural analysis, modelling and cell biology to define a regulated seipin conformational transition at the ER–lipid-droplet interface.

• Fung H.K.H.*, Hayashi Y.*, Salo V.T.*, Babenko A., Zagoriy I., Brunner A., Ellenberg J., Müller C.W., Cuylen-Haering S., Mahamid J.
  Genetically encoded multimeric tags for subcellular protein localisation in cryo-EM.
  Nature Methods 20, 1900–1908 (2023).
  10.1038/s41592-023-02053-0
  Developed cryo-compatible multimeric tagging tools enabling precise in-cell protein localisation for cryo-ET.

• Combot Y.*, Salo V.T.*, Chadeuf G., Hölttä M., Ven K., Pulli I., Ducheix S., et al.
  Seipin localizes at endoplasmic-reticulum–mitochondria contact sites to control mitochondrial calcium import and metabolism in adipocytes.
  Cell Reports 38(2): 110213 (2022).
  10.1016/j.celrep.2021.110213
  Identified a role for seipin in coordinating calcium flux at ER–mitochondria contact sites.

• Prasanna X.*, Salo V.T.*, Li S., Ven K., Vihinen H., Jokitalo E., Vattulainen I., Ikonen E.
  Seipin traps triacylglycerols to facilitate their nanoscale clustering in the endoplasmic-reticulum membrane.
  PLOS Biology 19(1): e3000998 (2021).
  10.1371/journal.pbio.3000998
  Combined simulations and in-cell imaging to describe how seipin promotes initial lipid droplet nucleation in the ER.

• Santinho A., Salo V.T., Chorlay A., Li S., Zhou X., Omrane M., Ikonen E., Thiam A.R.
  Membrane curvature catalyzes lipid droplet assembly.
  Current Biology 30(13): 2481–2494.e6 (2020).
  10.1016/j.cub.2020.04.066
  Uncovered a role for ER membrane architecture in regulating lipid droplet assembly.

• Salo V.T.*, Li S.*, Vihinen H., Hölttä-Vuori M., Szkalisity A., Horvath P., et al.
  Seipin facilitates triglyceride flow to lipid droplets and counteracts droplet ripening via endoplasmic-reticulum contact.
  Developmental Cell 50(4): 478–493.e9 (2019).
  10.1016/j.devcel.2019.05.016
  Demonstrated that seipin promotes neutral-lipid transfer within the ER to support lipid droplet growth.

• Salo V.T., Belevich I., Li S., Karhinen L., Vihinen H., Vigouroux C., Magré J., Thiele C., Hölttä-Vuori M., Jokitalo E., Ikonen E.
  Seipin regulates ER–lipid-droplet contacts and cargo delivery.
  EMBO Journal 35(24): 2699–2716 (2016).
  10.15252/embj.201695170
  Early work that revealed how seipin helps organize ER–lipid-droplet contact sites to control ER–LD cargo flux.

Full publication list

Pre-prints

• Salo V.T.*, Klug Y.A.*, Sapia J.*, Deme J.C., Tocci J.M., Babenko A., Jacob R.S., Eikmeier N., Zagoriy E., Goetz S.K., Campomanes P., Banterle N., Lea S.M., Vanni S., Carvalho P., Mahamid J.
  Regulated conformational transitions in seipin define a functional ER–lipid droplet interface.
  bioRxiv (2026).
  10.64898/2026.06.22.733769

• Sapia J., Salo V.T., Tasnim A.T., Campomanes P., Sui X., Vanni S.
  Substrate-dependent oligomerization modulates DGAT1 activity and subcellular localization.
  bioRxiv (2026).
  10.64898/2026.03.31.715571

First-author peer-reviewed research articles

• Fung H.K.H.*, Hayashi Y.*, Salo V.T.*, et al.
  Nature Methods (2023).
  10.1038/s41592-023-02053-0

• Combot Y.*, Salo V.T.*, et al.
  Cell Reports (2022).
  10.1016/j.celrep.2021.110213

• Prasanna X.*, Salo V.T.*, et al.
  PLOS Biology (2021).
  10.1371/journal.pbio.3000998

• Salo V.T.*, Li S.*, et al.
  Developmental Cell (2019).
  10.1016/j.devcel.2019.05.016

• Salo V.T., Belevich I., et al.
  EMBO Journal (2016).
  10.15252/embj.201695170

• Hölttä-Vuori M.*, Salo V.T.*, et al.
  Human Molecular Genetics (2013).
  10.1093/hmg/dds518

Other peer-reviewed research articles

• Gemin O., Armijo V., Lecomte L., et al., Salo V.T., et al.
  EasyGrid: a versatile platform for automated cryo-EM sample preparation and quality control.
  Nature Methods (2026).
  10.1038/s41592-026-03127-5

• Nähse V., Raiborg C., Tan K.W., Mørk S., Torgersen M.L., Wenzel E.M., Nager M., Salo V.T., Johansen T., Ikonen E., Schink K.O., Stenmark H.
  ATPase activity of DFCP1 controls selective autophagy.
  Nature Communications 14: 4051 (2023).
  10.1038/s41467-023-39641-9

• Dumesnil C., Vanharanta L., Prasanna X., Omrane M., Carpentier M., Bhapkar A., Enkavi G., Salo V.T., Vattulainen I., Ikonen E., Thiam A.R.
  Cholesterol esters form supercooled lipid droplets whose nucleation is facilitated by triacylglycerols.
  Nature Communications 14: 915 (2023).
  10.1038/s41467-023-36375-6

• Long M., Sanchez-Martinez A., Longo M., Suomi F., Stenlund H., Johansson A.I., Ehsan H., Salo V.T., Montava-Garriga L., Naddafi S., Ikonen E., Ganley I.G., Whitworth A.J., McWilliams T.G.
  DGAT1 activity synchronises with mitophagy to protect cells from metabolic rewiring by iron depletion.
  EMBO Journal 41(10): e109390 (2022).
  10.15252/embj.2021109390

• Santinho A., Salo V.T., Chorlay A., Li S., Zhou X., Omrane M., Ikonen E., Thiam A.R.
  Membrane curvature catalyzes lipid droplet assembly.
  Current Biology 30(13): 2481–2494.e6 (2020).
  10.1016/j.cub.2020.04.066

• Li S., Prasanna X., Salo V.T., Vattulainen I., Ikonen E.
  An efficient auxin-inducible degron system with low basal degradation in human cells.
  Nature Methods 16(9): 866–869 (2019).
  10.1038/s41592-019-0512-x

• Pfisterer S.G., Gateva G., Horvath P., Pirhonen J., Salo V.T., Karhinen L., Varjosalo M., Ryhänen S.J., Lappalainen P., Ikonen E.
  Role for formin-like 1–dependent acto-myosin assembly in lipid droplet dynamics and lipid storage.
  Nature Communications 8: 14858 (2017).
  10.1038/ncomms14858

Reviews and commentaries

• Dudka W., Salo V.T.*, Mahamid J.
  Zooming into lipid droplet biology through the lens of electron microscopy.
  FEBS Letters 598(10): 1127–1142 (2024).
  10.1002/1873-3468.14899

• Salo V.T.*
  Seipin: still a mysterious protein?
  Frontiers in Cell and Developmental Biology 11: 1112954 (2023).
  10.3389/fcell.2023.1112954

• Salo V.T., Hölttä-Vuori M., Ikonen E.
  Seipin-mediated contacts as gatekeepers of lipid flux at the endoplasmic reticulum–lipid droplet nexus.
  Contact 3: 1–16 (2020).
  10.1177/2515256420945820

• Salo V.T., Ikonen E.
  Moving out but keeping in touch: contacts between endoplasmic reticulum and lipid droplets.
  Current Opinion in Cell Biology 57: 64–70 (2019).
  10.1016/j.ceb.2018.11.002