• Publications
  • Influence
Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle.
The literature that links coat proteins to vesicle targeting events is discussed and a role for the coat in directing a vesicles to its correct intracellular destination is revealed. Expand
Structure of the reovirus core at 3.6 Å resolution
Analysis of the reovirus core by X-ray crystallography shows that there are alternative, specific and completely non-equivalent contacts made by several surfaces of two of its proteins; that the RNA capping and export apparatus is a hollow cylinder, which probably sequesters its substrate to ensure completion of the capping reactions. Expand
The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering Complexes
It is proposed that TRAPPI facilitates nucleotide exchange primarily by stabilizing the nucleotide-binding pocket of Ypt1p in an open, solvent-accessible form and implies that TRAPPII activates YPT1p by an identical mechanism. Expand
Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer.
The structure revealed that tapasin interacts with both ERp57 catalytic domains, accounting for the stability of the heterodimer, and provided an example of a protein disulfide isomerase family member interacting with substrate. Expand
Structure of a lipid-bound Extended-Synaptotagmin indicates a role in lipid transfer
Structural analysis complemented by mass spectrometry revealed the presence of glycerophospholipids in the E- SYT2 SMP channel, indicating a direct role for E-SYTs in lipid transport, providing strong evidence for a role of SMP-domain-containing proteins in the control of lipid transfer at membrane contact sites. Expand
The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif
The structural results and experimental observations concerning the interaction between Exo70p and other exocyst subunits or Rho3p GTPase are consistent with an architecture wherein exocySt subunits are composed of mostly helical modules strung together into long rods. Expand
VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites
It is shown that the N-terminal portion of VPS13 is tubular, with a hydrophobic cavity that can solubilize and transport glycerolipids between membranes, implicating defects in membrane lipid homeostasis in neurological disorders resulting from their mutations. Expand
TRAPP complexes in membrane traffic: convergence through a common Rab
Advances illustrate how the TRAPP complexes link Ypt1 and RAB1 activation to distinct membrane-tethering events. Expand
Control of plasma membrane lipid homeostasis by the extended synaptotagmins
The formation of E-Syt-dependent ER–PM tethers in response to stimuli that cleave PtdIns(4,5)P2 and elevate Ca2+ may help reverse accumulation of diacylglycerol in the PM by transferring it to the ER for metabolic recycling. Expand
The EM structure of the TRAPPIII complex leads to the identification of a requirement for COPII vesicles on the macroautophagy pathway
  • D. Tan, Yiying Cai, +6 authors T. Walz
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences
  • 11 November 2013
Evidence is provided that COPII-coated vesicles and the ER-Golgi fusion machinery are needed for macroautophagy, and the single-particle electron microscopy structure of TRAPPIII reveals that the dome-shaped Trs85 subunit associates primarily with the Trs20 subunit of TRAPPI. Expand