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Related Experiment Videos

How Tlg2p/syntaxin 16 'snares' Vps45.

Irina Dulubova1, Tomohiro Yamaguchi, Yan Gao

  • 1Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.

The EMBO Journal
|July 12, 2002
PubMed
Summary
This summary is machine-generated.

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Soluble NSF Attachment Protein Receptors (SNAREs) and SM proteins mediate membrane fusion. This study reveals SNAREs do not require a closed conformation for SM protein binding, uncovering a widespread conserved mechanism.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Soluble NSF Attachment Protein Receptors (SNAREs) and Sec1p/Munc18-homologs (SM proteins) are crucial for intracellular membrane fusion.
  • The precise mechanism coupling SNARE complex assembly to SM protein function remains incompletely understood.
  • Previous models suggested yeast trans-Golgi network/endosomal SNARE complex assembly requires SM protein Vps45p binding to a closed conformation of syntaxin Tlg2p.

Purpose of the Study:

  • To investigate the structural basis of Tlg2p and Pep12p syntaxin interaction with SM protein Vps45p.
  • To elucidate the conserved mechanism of coupling SNAREs and SM proteins in intracellular membrane fusion.

Main Methods:

  • Nuclear magnetic resonance (NMR) spectroscopy.
  • Biochemical experiments.

Related Experiment Videos

  • Comparative analysis of yeast and mammalian syntaxin-SM protein interactions.

    • Main Results:

    • Yeast syntaxins Tlg2p and Pep12p, despite characteristic domain structures, do not adopt a closed conformation.
    • Tlg2p binds Vps45p via a specific N-terminal peptide motif, a mode conserved in mammalian syntaxin 16.
    • This binding mode is similar to interactions between SM protein Sly1p and syntaxins Ufe1p and Sed5p.

    Conclusions:

    • SNAREs do not require a closed conformation for interaction with SM proteins, challenging previous models.
    • A conserved N-terminal peptide motif mediates the widespread coupling mechanism between syntaxins and SM proteins.
    • This mechanism represents a conserved strategy for regulating intracellular membrane fusion across species.