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Vol. 10, Issue 4, 1001-1017, April 1999
§
*Department of Cell Biology and Myo2p is a yeast class V myosin that functions in membrane
trafficking. To investigate the function of the carboxyl-terminal-tail domain of Myo2p, we have overexpressed this domain behind the regulatable GAL1 promoter (MYO2DN).
Overexpression of the tail domain of Myo2p results in a
dominant-negative phenotype that is phenotypically similar to a
temperature-sensitive allele of myo2, myo2-66. The tail
domain of Myo2p is sufficient for localization at low- expression
levels and causes mislocalization of the endogenous Myo2p from sites of
polarized cell growth. Subcellular fractionation of polarized,
mechanically lysed yeast cells reveals that Myo2p is present
predominantly in a 100,000 × g pellet. The Myo2p
in this pellet is not solubilized by Mg++-ATP or Triton
X-100, but is solubilized by high salt. Tail overexpression does not
disrupt this fractionation pattern, nor do mutations in sec4,
sec3, sec9, cdc42, or myo2. These results show
that overexpression of the tail domain of Myo2p does not compete with
the endogenous Myo2p for assembly into a pelletable structure, but does
compete with the endogenous Myo2p for a factor that is necessary for
localization to the bud tip.
Department of
Pathology, Yale University School of Medicine, New Haven, Connecticut
06520; and §Department of Molecular, Cellular
Developmental Biology, Yale University, New Haven, Connecticut 06520
Corresponding author. E-mail address:
reckpesl{at}biomed.med.yale.edu.
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