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Andreas Ernst


Cells face a daunting logistical challenge, with thousands of reactions taking place each second to sustain their growth and viability. To address this challenge, eukaryotic cells organize their interior into a set of membrane-enclosed compartments, referred to as organelles or the endomembrane system. These compartments communicate via membranous carriers to exchange material (e.g. proteins and lipids). Importantly, each organelle has a unique biochemical composition, and exhibits both complex dynamics and a distinct morphology. How organelles are shaped, how their shape is linked to their functions, and how individual organelles engage in specific contacts are important questions that are the focus of our research.

We are specifically focused on the early secretory pathway, where two organelles, the ER and the Golgi stack, form a ‘synapse-like’ interface that is conserved across taxa. This junction functions as an ‘assembly line’, in which macromolecules (e.g. proteins and lipids) that are manufactured in the ER are shipped to the Golgi, and then processed and distributed to multiple locations within as well as outside of the cell. The ER-Golgi interface can be considered as a critical cellular ‘valve’ controlling the output of a large fraction of proteins encoded in the human genome. It is remarkable how this interface rapidly sorts components, maintains itself despite high membrane throughput, and yet rapidly disengages during transitions to mitosis or autophagy.

Our goal is to understand the mechanisms that establish the ER-Golgi interface and enable efficient processing and sorting of cargo within this space. We pursue a ‘bottom-up’ approach in which we purify individual components to homogeneity and probe them in a model membrane environment, seeking out the minimal components and mechanisms needed to reconstitute morphology and function. We complement this approach with super-resolution and electron microscopy, genetic perturbations and functional assays. Through this dual strategy, we hope to elucidate the principles by which the ER-Golgi interface is formed and maintained to execute its many critical cellular functions.


  • Ziltener, P.*, Rebane, A. A.*, Graham, M., Ernst, A. M. +, & Rothman, J. E. + (2020). The golgin family exhibits a propensity to form condensates in living cells. FEBS Letters, in press. PMID: 32668013.
  • Raote, I., Ernst, A. M., Campelo, F., Rothman, J. E., Pincet, F., & Malhotra, V. (2020). TANGO1 membrane helices create a lipid diffusion barrier at curved membranes. eLife, e57822. PMID: 32452385.
  • Rebane, A. A. *, Ziltener, P. *, LaMonica, L. C., Bauer, A. H., Zheng, H., López-Montero, I., Pincet, F., Rothman, J. E. +, & Ernst, A. M. + (2020). Liquid-liquid phase separation of the Golgi matrix protein GM130. FEBS Letters, 7, 1132–1144. PMID: 31833055.
  • Kilian, N. +, Zhang, Y., LaMonica, L., Hooker, G., Toomre, D., Mamoun, C. B. +, & Ernst, A. M. + (2020). Palmitoylated Proteins in Plasmodium falciparum-Infected Erythrocytes: Investigation with Click Chemistry and Metabolic Labeling. BioEssays: News and Reviews in Molecular, Cellular and Developmental Biology, 6, e1900145. PMID: 32342554.
  • Ernst, A. M. +, Toomre, D., & Bogan, J. S. (2019). Acylation - A New Means to Control Traffic Through the Golgi. Frontiers in Cell and Developmental Biology, 109. PMID: 31245373.
  • Ernst, A. M. +, Syed, S. A., Zaki, O., Bottanelli, F., Zheng, H., Hacke, M., Xi, Z., Rivera-Molina, F., Graham, M., Rebane, A. A., Björkholm, P., Baddeley, D., Toomre, D., Pincet, F., & Rothman, J. E. + (2018). S-Palmitoylation Sorts Membrane Cargo for Anterograde Transport in the Golgi. Developmental Cell, 4,479-493.e7. PMID: 30458139.
  • Dunlop, M. H., Ernst, A. M., Schroeder, L. K., Toomre, D. K., Lavieu, G., & Rothman, J. E. (2017). Land-locked mammalian Golgi reveals cargo transport between stable cisternae. Nature Communications, 1, 432. PMID: 28874656.
  • Bottanelli, F., Kilian, N., Ernst, A. M., Rivera-Molina, F., Schroeder, L. K., Kromann, E. B., Lessard, M. D., Erdmann, R. S., Schepartz, A., Baddeley, D., Bewersdorf, J., Toomre, D., & Rothman, J. E. (2017). A novel physiological role for ARF1 in the formation of bidirectional tubules from the Golgi. Molecular Biology of the Cell, 12, 1676–1687. PMID: 28428254.
  • Björkholm, P.*, Ernst, A. M.*, Hagström, E.*, & Andersson, S. G. (2016). Why mitochondria need a genome revisited. FEBS Letters, 1, 65–75. PMID: 27928819.
  • Covino, R., Ballweg, S., Stordeur, C., Michaelis, J. B., Puth, K., Wernig, F., Bahrami, A., Ernst, A. M., Hummer, G., & Ernst, R. (2016). A Eukaryotic Sensor for Membrane Lipid Saturation. Molecular Cell, 1, 49–59. PMID: 27320200.
  • Björkholm, P., Harish, A., Hagström, E., Ernst, A. M., & Andersson, S. G. (2015). Mitochondrial genomes are retained by selective constraints on protein targeting. Proceedings of the National Academy of Sciences of the United States of America, 33, 10154–10161. PMID: 26195779.
  • Hacke, M., Björkholm, P., Hellwig, A., Himmels, P., Ruiz de Almodóvar, C., Brügger, B., Wieland, F., & Ernst, A. M. + (2015). Inhibition of Ebola virus glycoprotein-mediated cytotoxicity by targeting its transmembrane domain and cholesterol. Nature Communications, 7688. PMID: 26158910
  • Björkholm, P.*, Ernst, A. M.*, Hacke, M., Wieland, F., Brügger, B., & von Heijne, G. (2014). Identification of novel sphingolipid-binding motifs in mammalian membrane proteins. Biochimica et Biophysica Acta, 8, 2066–2070. PMID: 24796501.
  • Ernst, A. M. +, & Brügger, B. + (2013). Sphingolipids as modulators of membrane proteins. Biochimica et Biophysica Acta, 5, 665–670. PMID: 24201378.
  • Swidergall, M., Ernst, A. M., & Ernst, J. F. (2013). Candida albicans mucin Msb2 is a broad-range protectant against antimicrobial peptides. Antimicrobial Agents and Chemotherapy, 8, 3917–3922. PMID: 23733470.
  • Ernst, A. M., Zacherl, S., Herrmann, A., Hacke, M., Nickel, W., Wieland, F. T., & Brügger, B. (2013). Differential transport of Influenza A neuraminidase signal anchor peptides to the plasma membrane. FEBS Letters, 9, 1411–1417.
  • Ernst, A. M., Contreras, F. X., Thiele, C., Wieland, F., & Brügger, B. (2012). Mutual recognition of sphingolipid molecular species in membranes. Biochimica et Biophysica Acta, 11, 2616–2622. PMID: 22699040
  • Contreras, F. X.*, Ernst, A. M.*, Haberkant, P., Björkholm, P., Lindahl, E., Gönen, B., Tischer, C., Elofsson, A., von Heijne, G., Thiele, C., Pepperkok, R., Wieland, F., & Brügger, B. (2012). Molecular recognition of a single sphingolipid species by a protein's transmembrane domain. Nature, 7382, 525–529.
  • Contreras, F. X., Ernst, A. M., Wieland, F., & Brügger, B. (2011). Specificity of intramembrane protein-lipid interactions. Cold Spring Harbor Perspectives in Biology, 6. PMID: 21536707.
  • Ernst, A. M. +, Contreras, F. X., Brügger, B., & Wieland, F. + (2010). Determinants of specificity at the protein-lipid interface in membranes. FEBS Letters, 9, 1713–1720. PMID: 20085759.

*: equal contribution, +: corresponding author


Andreas Max Ernst received his doctorate in biochemistry from Heidelberg University, Germany, working in the laboratory of Dr. Felix Wieland & Dr. Britta Brügger. He then joined the laboratory of Dr. James E. Rothman at Yale School of Medicine - first as a postdoctoral fellow, and later on as a research scientist. Andreas joined the Division of Biological Sciences faculty at U.C. San Diego in July 2020.