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Multiple sequence signals determine the distribution of glycosylphosphatidylinositol proteins between the plasma membrane and cell wall in Saccharomyces cerevisiae

¹ Department of Molecular Biology and Genetics and Program in Cellular, Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, USA
² Department of Molecular Medicine, Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, USA

Correspondence
Brendan P. Cormack
bcormack{at}bs.jhmi.edu

Glycosylphosphatidylinositol (GPI)-anchored cell wall proteins (GPI-CWPs) play an important role in the structure and function of the cell wall in Saccharomyces cerevisiae and other fungi. While the majority of characterized fungal GPI-anchored proteins localize to the cell wall, a subset of GPI proteins are thought to reside at the plasma membrane and not to traffic significantly to the cell wall. The amino acids immediately upstream of the site of GPI anchor addition (the site) are the primary signal determining whether a GPI protein localizes to the cell wall or to the plasma membrane. Here, evidence was found that in addition to this -proximal signal, other sequences in the protein can impact the distribution of GPI proteins between cell wall and membrane. In particular, it was found that long regions rich in serine and threonine residues (a feature of many cell wall proteins) can override the -proximal signal and redirect a model GPI plasma membrane protein to the cell wall.

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