Yongli Zhang
Yale University, CT·Biophysics
Cells constantly move material between membranes. Two complementary ways of doing so are fusing membranes together and passing lipids (fat molecules that make up membranes) directly from one membrane to another.
- Fields
Biophysics
Biochemistry
Neuroscience
- Topics
SNARE proteins
SNARE assembly
synaptic vesicle fusion
- Grants
- 1 known grant, through Apr 2029
What they work on
- Reconstitute the full primed SNARE complex, adding complexin and the calcium sensor synaptotagmin-1 to Munc18-1, syntaxin-1, VAMP2 and Munc13-1, and characterize its stability, structure and dynamics on membranes.
- Measure the dynamics of SNARE zippering that drives calcium-triggered synaptic vesicle fusion at the single-molecule level, using optical tweezers combined with fluorescence microscopy.
- Test whether gradients of membrane tension and membrane protein density drive the direction and rate of lipid flow through bridge lipid transfer proteins, using new lipid transfer assays.
More about the research
Faults in either pathway have been linked to many diseases. This project measures the forces behind both processes, one molecule at a time.
Why it matters
SNARE-driven membrane fusion and bridge-protein lipid transfer are central to how cells move material, and malfunctions in both have been linked to numerous diseases. Clarifying the forces and protein assemblies behind them, from neurotransmitter release to organelle growth, adds basic understanding. That understanding may eventually inform ways to intervene in these diseases.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Yann Chemla
University of Illinois Urbana-Champaign, IL·Biophysics
Determine how contacts with DNA and non-canonical DNA structures control the unwinding activity of the UvrD, Rep and XPD helicases, using optical tweezers combined with fluorescence microscopy.
John Peters
University of Richmond, VA·Neuroscience
Determine what the poorly characterized N-terminal and linker regions of SNAP-47, a SNARE membrane-fusion protein, contribute to vesicle fusion during AMPA receptor delivery, using an in vitro fusion assay with purified components.
Edwin R Chapman
University of Wisconsin-Madison, WI·Neuroscience
Measure opening, closing, widening and ion selectivity of single SNARE-formed fusion pores at microsecond resolution, using nanodiscs fused to an artificial lipid membrane and electrical recording.
The school
Yale University: 73 labs on PI Pages, $1.5B a year on research, 438 research doctorates a year.
Reach out
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