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Related Concept Videos

Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Cotranslational Protein Translocation01:20

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Conjugative Mating Assays for Sequence-specific Analysis of Transfer Proteins Involved in Bacterial Conjugation
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TRAPP II complex assembly requires Trs33 or Trs65.

Andrei A Tokarev1, David Taussig, Geetanjali Sundaram

  • 1Department of Biological Sciences, Laboratory for Molecular Biology, University of Illinois at Chicago, Molecular Biology Research Building, 900 South Ashland Avenue Chicago, IL 60607, USA.

Traffic (Copenhagen, Denmark)
|October 22, 2009
PubMed
Summary
This summary is machine-generated.

The TRAPP II complex assembly requires either Trs33 or Trs65, two related subunits. This finding in yeast suggests a conserved mechanism for TRAPP II assembly in humans.

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Published on: January 4, 2017

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Complexes

Background:

  • The TRAPP complex is a Ypt/Rab activator crucial for Golgi apparatus function.
  • TRAPP II, a distinct form, includes essential subunits Trs120 and Trs130.
  • Trs65, a fungi-specific subunit, was previously implicated in TRAPP II assembly.

Purpose of the Study:

  • To investigate the function of the conserved TRAPP subunit, Trs33.
  • To determine the role of Trs33 in TRAPP II assembly.
  • To explore the functional relationship between Trs33 and Trs65.

Main Methods:

  • Genetic interaction studies between Trs33 and TRAPP II subunits.
  • Physical interaction assays to confirm Trs33 binding.
  • Analysis of TRAPP II levels and Golgi Ypt localization in trs33 mutants.

Main Results:

  • Trs33 and Trs65 share similarities in sequence, localization, and interaction.
  • Trs33 interacts genetically with Trs120 and Trs130, and physically with Trs120.
  • trs33 mutant cells show reduced TRAPP II levels and mislocalized Golgi Ypts.

Conclusions:

  • Trs33 is essential for TRAPP II assembly in yeast, acting redundantly with Trs65.
  • The assembly of TRAPP II can be achieved by either Trs33 or Trs65.
  • The essential role of Trs33 in TRAPP II assembly is likely conserved in humans, given the presence of Trs33 homologues.