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Published online 7 August 2000. doi:10.1083/jcb.150.3.513
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© The Rockefeller University Press, 0021-9525/2000//513 $5.00
The Journal of Cell Biology, Volume 150, Number 3, , 2000 513-526

Original Article

Two Distinct Regions in a Yeast Myosin-V Tail Domain Are Required for the Movement of Different Cargoes



Natalie L. Catletta, Jason E. Duexa, Fusheng Tanga, and Lois S. Weismana

a Department of Biochemistry, University of Iowa, Iowa City, Iowa 52242
Department of Biochemistry, University of Iowa, Iowa City, IA 52242.(319) 335-9570(319) 335-8581

lois-weisman{at}uiowa.edu

The Saccharomyces cerevisiae myosin-V, Myo2p, is essential for polarized growth, most likely through transport of secretory vesicles to the developing bud. Myo2p is also required for vacuole movement, a process not essential for growth. The globular region of the myosin-V COOH-terminal tail domain is proposed to bind cargo. Through random mutagenesis of this globular tail, we isolated six new single point mutants defective in vacuole inheritance, but not polarized growth. These point mutations cluster to four amino acids in an 11-amino acid span, suggesting that this region is important for vacuole movement. In addition, through characterization of myo2-{Delta}AflII, a deletion of amino acids 1,459–1,491, we identified a second region of the globular tail specifically required for polarized growth. Whereas this mutant does not support growth, it complements the vacuole inheritance defect in myo2-2 (G1248D) cells. Moreover, overexpression of the myo2-{Delta}AflII globular tail interferes with vacuole movement, but not polarized growth. These data indicate that this second region is dispensable for vacuole movement. The identification of these distinct subdomains in the cargo-binding domain suggests how myosin-Vs can move multiple cargoes. Moreover, these studies suggest that the vacuole receptor for Myo2p differs from the receptor for the essential cargo.

Key Words: organelle movement • vacuole • molecular motor • Myo2p • Saccharomyces cerevisiae

© 2000 The Rockefeller University Press

Abbreviations used in this paper: CPY, carboxypeptidase Y; FM4-64, N-(3-triethylammoniumpropyl)-4-(6(4-(diethylamino)phenyl)hexatrienyl) pyridinium dibromide; PrB, proteinase B; YEPD, 1% yeast extract, 2% peptone, 2% dextrose.


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