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First published online 20 January 2004
doi: 10.1242/jcs.00897

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Phosphorylation of golgin-160 by mixed lineage kinase 3

¹ Department of Pharmaceutical Sciences, University of Maryland-School of Pharmacy, Baltimore, MD 21201, USA
² Department of Cell Biology, Johns Hopkins University-School of Medicine, Baltimore, MD 21205, USA
³ Department of Physiology, Michigan State University, East Lansing, MI 48824, USA

^* Author for correspondence (e-mail: pshapiro{at}rx.umaryland.edu)

Accepted 19 September 2003

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.

Key words: MAP kinase, Phosphorylation, Golgi complex, Golgins, Caspase

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