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Study of Protein-protein Interactions in Autophagy Research
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TRAPP Complexes in Secretion and Autophagy.

Jane J Kim1, Zhanna Lipatova2, Nava Segev2

  • 1Department of Biological Sciences, University of Illinois at Chicago Chicago, IL, USA.

Frontiers in Cell and Developmental Biology
|April 12, 2016
PubMed
Summary
This summary is machine-generated.

The TRAPP complex, crucial for intracellular transport, acts as a Ypt/Rab GTPase nucleotide exchanger. New insights reveal its roles in secretion and autophagy, with potential direct functions in vesicle tethering.

Keywords:
GEFGTPaseRabYptautophagysecretiontether

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Complexes

Background:

  • TRAPP (Transport Protein Particle) is a conserved multi-subunit complex.
  • Initially identified for ER-to-Golgi transport, its role as a Ypt/Rab GTPase GEF was established.
  • Three TRAPP complexes (I, II, III) in yeast regulate secretion and autophagy.

Purpose of the Study:

  • To review recent advancements in understanding TRAPP complex function.
  • To highlight new insights into TRAPP's roles in intracellular trafficking.
  • To discuss current controversies and future research directions.

Main Methods:

  • Characterization of TRAPP subunit composition and assembly.
  • Analysis of TRAPP's GTPase nucleotide exchange factor (GEF) activity.
  • Investigating TRAPP interactions with vesicle coat components.

Main Results:

  • Core TRAPP self-assembles and exhibits GEF activity on Ypt1.
  • Trs20/Sedlin acts as an adaptor for TRAPP II and III formation.
  • The architecture of larger TRAPP complexes and their potential direct role in vesicle tethering are under investigation.

Conclusions:

  • TRAPP complexes are essential regulators of diverse intracellular trafficking pathways.
  • Further research is needed to clarify the structure and direct functions of larger TRAPP complexes.
  • Understanding TRAPP is critical, given its links to human diseases.