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Related Experiment Video

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Structure and function of longin SNAREs.

Frédéric Daste1, Thierry Galli1, David Tareste2

  • 1Université Paris Diderot, Sorbonne Paris Cité, Institut Jacques Monod, CNRS UMR 7592, Membrane Traffic in Health & Disease, INSERM ERL U950, Paris F-75013, France.

Journal of Cell Science
|November 15, 2015
PubMed
Summary
This summary is machine-generated.

The longin domain, a part of Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins, acts as a key regulator in membrane trafficking. It controls SNARE protein localization and fusion activity, impacting intracellular transport and communication.

Keywords:
Lipid transferLonginMembrane proteinsSNAREVesicular trafficking

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins are essential for membrane fusion in intracellular transport and communication.
  • The long N-terminal domain (longin domain) of certain SNAREs was proposed as a regulator of membrane trafficking over a decade ago.

Purpose of the Study:

  • To review structure-function data on prototypical longin SNAREs (Ykt6, VAMP7, Sec22b) over the past decade.
  • To highlight conserved mechanisms of longin domain regulation in SNARE function.

Main Methods:

  • Review of structural, biochemical, and cell biology studies.
  • Analysis of conserved molecular mechanisms.

Main Results:

  • The longin domain regulates SNARE sorting and activity.
  • Longin domains can inhibit membrane fusion by folding onto the SNARE coiled-coil domain.
  • Interactions with regulatory proteins influence intracellular sorting of longin SNAREs.

Conclusions:

  • The longin domain possesses a dual function, regulating both membrane localization and fusion activity of SNAREs.
  • This dual role establishes the longin domain as a critical regulatory module in intracellular trafficking.