THESIS
2021
1 online resource (xiii, 110 pages) : illustrations (some color)
Abstract
Glycosylphosphatidylinositol-anchored proteins (GPI-AP) are the primary protein
components of yeast cell wall and thus, essential for cellular integrity. The targeting of GPIAPs
to the cell surface requires extensive remodeling of the GPI anchor. It has been generally
accepted that remodeling of the GPI anchor is exclusively carried out in the Endoplasmic
reticulum (ER) in yeast cells, including the addition and subsequent removal of ethanolamine
phosphate (EtNP) from mannose 1 (Man1) and mannose 2 (Man2) of the glycan moiety.
My study provides evidence that the removal of EtNP from Man2 is essential for cell
viability and is mediated by Ted1p in the ER and Dcr2p in the Golgi. Moreover, I also establish
that Cdc1p, which was previously reported to be an ER-resident remodelase, is in fac...[
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Glycosylphosphatidylinositol-anchored proteins (GPI-AP) are the primary protein
components of yeast cell wall and thus, essential for cellular integrity. The targeting of GPIAPs
to the cell surface requires extensive remodeling of the GPI anchor. It has been generally
accepted that remodeling of the GPI anchor is exclusively carried out in the Endoplasmic
reticulum (ER) in yeast cells, including the addition and subsequent removal of ethanolamine
phosphate (EtNP) from mannose 1 (Man1) and mannose 2 (Man2) of the glycan moiety.
My study provides evidence that the removal of EtNP from Man2 is essential for cell
viability and is mediated by Ted1p in the ER and Dcr2p in the Golgi. Moreover, I also establish
that Cdc1p, which was previously reported to be an ER-resident remodelase, is in fact localized
to cis/medial Golgi. In summary, my thesis research establishes that EtNP is removed from
Man1 and Man2 of GPI-APs in the Golgi (via Cdc1p and Dcr2p), and while these enzymes
rely on COPI-coatomer function for their steady-state localization to the Golgi, they do not
ordinarily cycle between the Golgi and the ER.
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