The Henne Lab is interested in how cells spatially organize their metabolism. This includes understanding how cells adapt to nutritional stress, and remodel their organelles to survive. Armed with this knowledge, we also hope to deeply understand molecular mechanisms that govern human physiology and disease. 

One current focus is understanding how cells store lipids in lipid droplets (LDs), and use LDs to maintain homeoatasis. LDs do not work in isolation, and much of the lab is dedicated to chatacterizing how LDs form contacts with other cellular organelles. We are also interested in how cells spatially and functionally organize their LD stores to balance long-term lipid storage with efficient mobilization during energetic crises. 

Recently, we characterized a new protein family (the PXA domain-containing family) that plays critical roles in LD biogenesis and LD spatial organization within the cell. Budding yeast encode a PXA domain-containing protein called Mdm1 that we found acts as a "molecular tether" connecting LDs to the yeast lysosome/vacuole (Henne, JCB, 2015; Hariri, EMBO reports, 2017; Hariri, JCB, 2019). Mdm1 is highly conserved in metazoans, and we also found that its human homolog SNX14 regulates LD growth and homeostasis, which is perturbed in the genetic neurological disease SCAR20 (Bryant, HMG, 2018; Datta, JCB, 2019). The Drosophila fruit fly also encodes a Mdm1 homolog called Snazarus (Snz), which we discovered localizes to ER-PM contact sites in Drosophila adipocytes and regulates a sub-population of peripheral LDs (Ugrankar, Dev Cell, 2019).  Thus, PXA domain-containing proteins appear to function as "metabolic tethers" that regulate LD biogenesis as well as LD attachment to other cellular compartments, thus controlling LD spatial organization and the interactions LDs have with other organelles.

Background: Dr. Henne received his B.S. in Cellular and Molecular Biology from Texas Tech University in Lubbock, Texas, and then accepted a MRC Scholarship from the UK to pursue graduate studies at the MRC Laboratory of Molecular Biology at Cambridge University. As a student in the lab of Harvey McMahon, Ph.D., he studied how membrane sculpting BAR and F-BAR domain-containing proteins promote clathrin-mediated endocytosis. He characterized the F-BAR proteins FCHo1/2, and showed that they play crucial roles initiating clathrin vesicle biogenesis. Mike was awarded the Max Perutz Prize for his graduate work.

Following graduate school, Dr. Henne began a postdoctoral position in the laboratory of Scott Emr, Ph.D., at Cornell University as a Sam and Nancy Fleming Research Fellow. There, he continued to study endolysosomal trafficking, and how endosomes can be reshaped by the ESCRT (Endosomal Sorting Complexes Required for Transport) pathway. His work has focused on reconstituting and imaging ESCRT protein assemblies, and dissecting how they shape multi-vesicular endosomes. More recent projects involve global screens in yeast to identify novel proteins involved in endolysosomal trafficking.

Dr. Henne uses cell biology, biochemistry, structural biology, and genetics to understand the molecular mechanisms of LD dynamics, and the spatial organization of cellular lipid metabolism. 

Research Interest

  • inter-organelle communication
  • lipid metabolism
  • membrane sculpting


Featured Publications LegendFeatured Publications

Endoplasmic Reticulum-Vacuole Contact Sites "Bloom" With Stress-Induced Lipid Droplets.
Henne WM, Hariri H Contact (Thousand Oaks) 2018 Jan-Dec 1
larval feeding through insulin signaling and SLC5A11.
Ugrankar R, Theodoropoulos P, Akdemir F, Henne WM, Graff JM Commun Biol 2018 1 110
Discovery and Roles of ER-Endolysosomal Contact Sites in Disease.
Henne WM Adv. Exp. Med. Biol. 2017 997 135-147
Inter-organelle ER-endolysosomal contact sites in metabolism and disease across evolution.
Hariri H, Ugrankar R, Liu Y, Henne WM Commun Integr Biol 2016 May-Jun 9 3 e1156278
ESCRT-III activation by parallel action of ESCRT-I/II and ESCRT-0/Bro1 during MVB biogenesis.
Tang S, Buchkovich NJ, Henne WM, Banjade S, Kim YJ, Emr SD Elife 2016 Apr 5
Structural basis for activation, assembly and membrane binding of ESCRT-III Snf7 filaments.
Tang S, Henne WM, Borbat PP, Buchkovich NJ, Freed JH, Mao Y, Fromme JC, Emr SD Elife 2015 Dec 4
Molecular mechanisms of inter-organelle ER-PM contact sites.
Henne WM, Liou J, Emr SD Curr. Opin. Cell Biol. 2015 May 35 123-130
Essential N-terminal insertion motif anchors the ESCRT-III filament during MVB vesicle formation.
Buchkovich NJ, Henne WM, Tang S, Emr SD Dev. Cell 2013 Oct 27 2 201-14
Molecular mechanisms of the membrane sculpting ESCRT pathway.
Henne WM, Stenmark H, Emr SD Cold Spring Harb Perspect Biol 2013 Sep 5 9
The endosomal sorting complex ESCRT-II mediates the assembly and architecture of ESCRT-III helices.
Henne WM, Buchkovich NJ, Zhao Y, Emr SD Cell 2012 Oct 151 2 356-71

Honors & Awards

  • Searle Scholar
  • Sam & Nancy Fleming Research Fellowship
  • The Max Perutz Prize
    awarded for Graduate work at MRC, Cambridge, UK (2009)