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Role of Mammalian coronin 7 in the biosynthetic pathway

Vasily Rybakin1

  • 1The Scripps Research Institute, 10550 N Torrey Pines Road, La Jolla, CA 92037, USA. vrybakin@scripps.edu

Sub-Cellular Biochemistry
|October 18, 2008
PubMed

Insights

Mammalian coronin 7 protein, unlike other coronins, binds to Golgi membranes. It mediates cargo vesicle formation at the trans-Golgi network (TGN), crucial for protein export.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Interactions

Background:

  • Most coronin proteins interact with actin for their cellular functions.
  • Mammalian coronin 7 has a distinct role, localizing to the Golgi complex membranes.
  • Its precise function and interactions within the Golgi were not well-defined.

Purpose of the Study:

  • To investigate the function of mammalian coronin 7.
  • To elucidate the molecular mechanisms underlying coronin 7's role in the Golgi complex.
  • To determine coronin 7's interaction partners and its involvement in protein trafficking.

Main Methods:

  • Utilized RNA interference (RNAi) to deplete coronin 7.
  • Investigated protein interactions using in vivo and in vitro assays.
  • Examined Golgi structure and cargo protein accumulation.

Main Results:

  • Coronin 7 localizes to the Golgi and requires Src kinase and AP-1 adaptor protein complex for targeting.
  • Coronin 7 interacts with and is phosphorylated by Src kinase.
  • Depletion of coronin 7 leads to Golgi breakdown and accumulation of arrested cargo proteins.

Conclusions:

  • Coronin 7 functions in the late stages of cargo sorting and export from the Golgi complex.
  • Coronin 7 acts as a mediator for cargo vesicle formation at the trans-Golgi network (TGN).
  • Its function is downstream of AP-1 cargo interaction and upstream of protein kinase D-dependent membrane fission.

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