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Vol. 15, Issue 3, 1397-1406, March 2004

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The Yeast Casein Kinase Yck3p Is Palmitoylated, then Sorted to the Vacuolar Membrane with AP-3-dependent Recognition of a YXX Adaptin Sorting Signal

Beimeng Sun ^*, Linyi Chen ^* , Wei Cao ^*, Amy F. Roth , and Nicholas G. Davis ^*  

^* Department of Pharmacology, Wayne State University School of Medicine, Detroit, Michigan 48201; Department of Surgery, Wayne State University School of Medicine, Detroit, Michigan 48201

Submitted September 19, 2003; Revised October 30, 2003; Accepted October 31, 2003
Monitoring Editor: Howard Riezman

Our previous work found the two yeast plasma membrane-localized casein kinases Yck1p and Yck2p to be palmitoylated on C-terminal Cys-Cys sequences by the palmitoyl transferase Akr1p. The present work examines a third casein kinase, Yck3p, which ends with the C-terminal sequence Cys-Cys-Cys-Cys-Phe-Cys-Cys-Cys. Yck3p is palmitoylated and localized to the vacuolar membrane. While the C-terminal cysteines are required for this palmitoylation, Akr1p is not. Palmitoylation requires the C-terminal Yck3p residues 463-524, whereas information for vacuolar sorting maps to the 409-462 interval. Vacuolar sorting is disrupted in cis through deletion of the 409-462 sequences and in trans through mutation of the AP-3 adaptin complex; both cis- and trans-mutations result in Yck3p missorting to the plasma membrane. This missorted Yck3p restores 37°C viability to yck1 yck2-ts cells. yck1 yck2-ts suppressor mutations isolated within the YCK3 gene identify the Yck3p vacuolar sorting signal—the tetrapeptide YDSI, a perfect fit to the YXX adaptin-binding consensus. Although YXX signals have a well-appreciated role in the adaptin-mediated sorting of mammalian cells, this is the first signal of this class to be identified in yeast.

Present address: Department of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, MI 48109.

Corresponding author. E-mail address: ndavis{at}genetics.wayne.edu.

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