Fungal yapsins and cell wall: a unique family of aspartic peptidases for a distinctive cellular function

• Published in: FEMS yeast research 2006-11, Vol.6 (7), p.966-978
• Main Authors: Gagnon-Arsenault, Isabelle, Tremblay, Jessy, Bourbonnais, Yves
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Aspartic Acid Endopeptidases - chemistry; Aspartic Acid Endopeptidases - genetics; Aspartic Acid Endopeptidases - physiology; aspartic peptidase; Cell Wall - chemistry; Cell walls; cell‐wall integrity; Enzyme Precursors - metabolism; Fungi; Fungi - enzymology; GPI‐anchor; Molecular Sequence Data; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - physiology; signalling pathways; yapsin; Yeast; zymogen activation
• ISSN: 1567-1356; 1567-1364
• DOI: 10.1111/j.1567-1364.2006.00129.x

A novel class of aspartic peptidases known as fungal yapsins, whose first member ScYps1p was identified more than a decade ago in Saccharomyces cerevisiae, is characteristically modified by the addition of a glycophosphatidylinositol moiety and has a preference for cleaving substrates C-terminally to mono- and paired-basic residues. Over the years, several other members, first in S. cerevisiae and then in other fungi, have been identified. The implication of fungal yapsins in cell-wall assembly and/or remodelling had been suspected for many years. However, it is only very recently that studies performed on S. cerevisae and Candida albicans have confirmed their importance for cell-wall integrity. Here, we review 16 years of research, covering all fundamental aspects of these unique enzymes, in an effort to track their functional significance. We also propose a nomenclature for fungal yapsins based on their sequence identity with the founding members of this family, the S. cerevisiae yapsins.