A novel phospholipid-binding protein from the yeast Saccharomyces cerevisiae 
with dual binding specificities for the transport GTPase Ypt7p and the Sec 
1-related Vps33p

Lazar, T.; Scheglmann, D.; Gallwitz, D.

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A novel phospholipid-binding protein from the yeast Saccharomyces cerevisiae with dual binding specificities for the transport GTPase Ypt7p and the Sec 1-related Vps33p

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Lazar, T.
Department of Molecular Genetics, MPI for biophysical chemistry, Max Planck Society;

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Gallwitz, D.
Department of Molecular Genetics, MPI for biophysical chemistry, Max Planck Society;

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Citation

Lazar, T., Scheglmann, D., & Gallwitz, D. (2002). A novel phospholipid-binding protein from the yeast Saccharomyces cerevisiae with dual binding specificities for the transport GTPase Ypt7p and the Sec 1-related Vps33p. European Journal of Cell Biology, 81(12), 635-646. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B7GJ2-4DPMBFV-C1-1&_cdi=20194&_user=38661&_pii=S0171933504702666&_orig=search&_coverDate=12%2F01%2F2002&_sk=999189987&view=c&wchp=dGLbVlW-zSkWA&md5=8802ddf9a7a7844db32f2bc4e33caad8&ie=/sdarticle.pdf.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-F276-E

Abstract

The gene product of the Saccharomyces cerevisiae open reading frame YDR229w (named IVY1 for: Interacting with Vps33p and Ypt7p) was found to interact with both the GTPase Ypt7p and the Sec1-related Vps33 protein. While deletion of IVY1 does not lead to any recognized change in phenotype, overexpression of Ivy1p leads to fragmentation of the vacuole, missorting of the vacuolar enzyme carboxypeptidase Y (CPY) to the exterior of the cell, and an accumulation of multivesicular bodies inside the cell. All effects caused by the overexpression of Ivy1p can be reset by simultaneously raising the amount of Vps33p. This suppression activity of Vps33p suggests that Ivv1p and Vps33p at least partially counteract the action of each other in the cell. The intracellular level of Ivy1p increases in cells approaching stationary growth phase at which part of the protein is located at the rim of the vacuole. In addition to its specific interactions with members of two regulatory protein families, Ivy1p in vitro shows a marked propensity for binding phospholipids with high affinity.