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

Yanzhuang Wang, Joachim Seemann, Marc Pypaert, James Shorter, Graham Warren

Research output: Contribution to journalArticlepeer-review

160 Scopus citations


Cell-free assays that mimic the disassembly and re-assembly cycle of the Golgi apparatus during mitosis implicated GRASP65 as a mitotically regulated stacking factor. We now present evidence that GRASP65 is directly involved in stacking Golgi cisternae. GRASP65 is the major phosphorylation target in rat liver Golgi membranes of two mitotic kinases, cdc2-cyclin B and polo-like kinases, which alone will unstack Golgi membranes, generating single cisternae. Mitotic cells microinjected with antibodies to GRASP65 fail to form proper Golgi stacks after cell division. Beads coated with GRASP65 homodimers form extensive aggregates consistent with the formation of trans oligomers. These can be disaggregated using purified cdc2-cyclin B1 and polo-like kinases, and re-aggregated after dephosphorylation of GRASP65. Together, these data demonstrate that GRASP65 has the properties required to bind surfaces together in a mitotically regulated manner.

Original languageEnglish (US)
Pages (from-to)3279-3290
Number of pages12
JournalEMBO Journal
Issue number13
StatePublished - Jul 1 2003


  • Golgi
  • Phosphorylation
  • Polo-like kinase
  • Stacking
  • cdc2 kinase

ASJC Scopus subject areas

  • General Neuroscience
  • Molecular Biology
  • General Biochemistry, Genetics and Molecular Biology
  • General Immunology and Microbiology


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