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Yeasts are single-celled organisms, but unlike bacteria, they are eukaryotes (cells with a nucleus). Cell signaling in yeast is similar to signaling in other eukaryotic cells. A ligand, such as a protein or a small molecule released from a yeast cell, attaches to a receptor on the cell surface. The binding stimulates second-messenger kinases to activate or inactivate transcription factors that further regulate gene expression. Many of the yeast intracellular signaling cascades have similar...
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Related Experiment Video

Updated: Dec 25, 2025

Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast
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Integrative structure and function of the yeast exocyst complex.

Sai J Ganesan1,2, Michael J Feyder3, Ilan E Chemmama1,2

  • 1Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, San Francisco, California, USA.

Protein Science : a Publication of the Protein Society
|April 3, 2020
PubMed
Summary

This study reveals the yeast exocyst complex architecture using integrative modeling. The findings clarify exocyst subunit positioning and dynamic conformations, advancing understanding of membrane trafficking mechanisms.

Keywords:
EMSNAREschemical cross-linking mass spectrometryexocytosisintegrative modelingmembrane fusionprotein cross-linkingstructural modelsyeast exocyst complex

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Molecular Mechanisms

Background:

  • The exocyst complex is an evolutionarily conserved, eight-subunit protein complex crucial for diverse membrane trafficking events.
  • It acts as a scaffold for key regulatory proteins, including small GTPases and SNAREs, to ensure accurate membrane fusion.
  • Despite its importance, the molecular-level mechanism and architecture of the exocyst remain incompletely understood.

Purpose of the Study:

  • To determine the molecular architecture of the yeast exocyst complex.
  • To integrate low-resolution structural data to build a comprehensive model.
  • To provide insights into exocyst subunit organization and dynamics.

Main Methods:

  • Integrative modeling combining negative-stain electron microscopy (EM) 3D density maps and chemical-crosslinking mass spectrometry (XL-MS) data.
  • Utilized disuccinimidyl suberate (DSS) and 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) cross-linking.
  • Validated the integrative model using existing cryo-electron microscopy (cryo-EM) structures and in vivo fluorescence microscopy.

Main Results:

  • An integrative model of the yeast exocyst complex architecture was established at ~16 Å resolution.
  • The model refined subunit configuration, placing Sec3 near Sec6, which was not evident in prior cryo-EM data.
  • Limited proteolysis indicated a dynamic conformation for the Exo70 subunit, suggesting functional flexibility.

Conclusions:

  • Integrative modeling with low-resolution structural data can generate testable hypotheses for biological mechanisms.
  • The refined exocyst architecture provides a framework for understanding its role in membrane tethering and fusion.
  • The dynamic nature of Exo70 may be critical for its interactions with SNAREs and membranes.