Phosphorylation of golgin-160 by mixed lineage kinase 3

Hyukjin Cha, Barbara L. Smith, Kathleen Gallo, Carolyn E. Machamer, Paulo Shapiro

Research output: Contribution to journalArticlepeer-review


Golgin-160 is a member of the coiled-coil family of golgin proteins, which are proposed to regulate the structure of the Golgi complex. The C-terminal two-thirds of golgin-160 is predicted to form a coiled-coil domain and the N-terminal head domain contains several putative binding domains, regulatory motifs and phosphorylation sites. Recently, it has been demonstrated that caspase-dependent cleavage of the golgin-160 head domain occurs rapidly after induction of apoptosis. The role of golgin-160 phosphorylation and the functional implications for Golgi structure have not been defined. In this study, we investigated the kinase(s) responsible for phosphorylation of golgin-160. Signaling through the small G-protein Rac and mixed-lineage-kinase-3 (MLK3) resulted in increased phosphorylation of golgin-160. The intracellular distribution of MLK3 overlapped with that of golgin-160 and the two proteins could be co-immunoprecipitated. In vitro kinase assays demonstrated that MLK3 directly phosphorylates golgin-160 in the N-terminal head region between residues 96 and 259. Overexpression of MLK3 caused an enhanced caspase-dependent cleavage of golgin-160 at Asp139. Golgin-160 is the first non-kinase substrate of MLK3 identified, and phosphorylation by MLK3 might modulate cleavage of golgin-160 during apoptosis.

Original languageEnglish (US)
Pages (from-to)751-760
Number of pages10
JournalJournal of cell science
Issue number5
StatePublished - Feb 15 2004


  • Caspase
  • Golgi complex
  • Golgins
  • MAP kinase
  • Phoshorylation

ASJC Scopus subject areas

  • Cell Biology


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