High impact information on ATC1

• These results strongly suggest that ATC1 is the structural gene encoding cell wall acid trehalase in C. albicans [1].
• The ATC1 gene encodes a cell wall-linked acid trehalase required for growth on trehalose in Candida albicans [1].
• Determinations of ATC1 mRNA expression as well as acid trehalase activity in the presence and absence of glucose point out that ATC1 gene is regulated by glucose repression [1].
• After screening a Candida albicans genome data base, the product of an open reading frame (IPF 19760/CA2574) with 41% identity to Saccharomyces cerevisiae vacuolar acid trehalase (Ath1p) was identified and named Atc1p [1].
• The deduced amino acid sequence shows that Atc1p contains an N-terminal hydrophobic signal peptide and 20 potential sites for N-glycosylation [1].

Biological context of ATC1

• However, loss of ATC1 in an arl1 background exacerbated ion sensitivities, although not the CPY phenotype [2].
• Lic4, a nuclear phosphoprotein that cooperates with calcineurin to regulate cation homeostasis in Saccharomyces cerevisiae [3].

Associations of ATC1 with chemical compounds

• Although loss of ARL1 confers several phenotypes, including sensitivity to hygromycin B and Li(+), reduced influx of K(+), and increased secretion of carboxypeptidase Y (CPY), loss of ATC1 was without effect by these and other measures [2].
• LIC4 (lithium comvertas) encodes a novel 33-kDa protein with no identity to known proteins [3].

Other interactions of ATC1

• Taken together, these observations suggest that calcineurin, Hal3, and Lic4 cooperatively regulate the response of yeast cells to cation stress [3].
• Here we identify two genes, PMR2B and LIC4 which, when overexpressed, suppress the cation-sensitive phenotype of yeast cells lacking calcineurin [3].

Analytical, diagnostic and therapeutic context of ATC1

• By indirect and direct immunofluorescence detection of HA- and GFP-tagged proteins, Lic4 is localized in the nucleus in wild-type cells but predominantly cytoplasmic in cells lacking calcineurin [3].

References