High impact information on ECM33

• Glycosylphosphatidylinositol-Anchored Ecm33p Influences Conidial Cell Wall Biosynthesis in Aspergillus fumigatus [1].
• Deletion of ECM33 leads to a weakened cell wall, and this defect is further aggravated by simultaneous deletion of PST1 [2].
• Ecm33p is a widely distributed fungal protein with functional relevance, clearly demonstrated by ecm33Delta mutant phenotypes, mainly related to the cell wall [3].
• Two ORFs, YBR0727 and YBR0745 most likely contain an intron [4].
• The localization change of Ybr078w/Ecm33, a yeast GPI-associated protein, from the plasma membrane to the cell wall, affecting the cellular function [5].

Biological context of ECM33

• Suppressors commonly effective to mpc1-4 and mpc1-5 mutations are PSD1, encoding phosphatidylserine decarboxylase, and ECM33, which were found to suppress the temperature-sensitive phenotype shown by the fsr2-1 and las21delta mutants, those of which have defects in the GPI anchor synthesis [6].
• Ecm33p, a GPI-anchored protein involved in cell wall biogenesis, has been found for the first time in lipid rafts [7].
• To identify potential mechanisms through which Ecm33p contributes to virulence, we investigated the interactions of C. albicans ecm33Delta mutants with endothelial cells and the FaDu oral epithelial cell line in vitro [8].

Anatomical context of ECM33

• Pst1p and Ecm33p are both localized to the cell surface, Pst1p being at the cell membrane and possibly also in the periplasmic space [2].

References