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Related Experiment Videos

A direct role for GRASP65 as a mitotically regulated Golgi stacking factor.

Yanzhuang Wang1, Joachim Seemann, Marc Pypaert

  • 1Department of Cell Biology, Ludwig Institute for Cancer Research, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA.

The EMBO Journal
|July 4, 2003
PubMed
Summary

GRASP65 is a key protein regulating Golgi apparatus stacking during cell division. Phosphorylation by mitotic kinases unstacks Golgi, while GRASP65 antibodies prevent proper stack formation.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The Golgi apparatus undergoes disassembly and reassembly during mitosis.
  • Identifying proteins that regulate Golgi structure during cell division is crucial.

Purpose of the Study:

  • To investigate the role of GRASP65 in Golgi cisternae stacking.
  • To determine if GRASP65 is a mitotically regulated stacking factor.

Main Methods:

  • Utilized cell-free assays mimicking Golgi dynamics.
  • Investigated the effect of mitotic kinases (cdc2-cyclin B, polo-like kinases) on Golgi membranes.
  • Microinjected mitotic cells with antibodies against GRASP65.
  • Used GRASP65-coated beads to study aggregation and disaggregation.

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Main Results:

  • GRASP65 is a major phosphorylation target of cdc2-cyclin B and polo-like kinases.
  • Mitotic kinase activity on GRASP65 leads to Golgi unstacking.
  • Antibodies to GRASP65 inhibit Golgi stack reformation post-mitosis.
  • GRASP65 homodimers form aggregates, which can be regulated by kinase activity and dephosphorylation.

Conclusions:

  • GRASP65 directly stacks Golgi cisternae.
  • GRASP65 functions as a mitotically regulated Golgi stacking factor.
  • GRASP65 possesses the properties to bind surfaces in a cell-cycle-dependent manner.