Fungal yapsins and cell wall: a unique family of aspartic peptidases for a distinctive cellular function.
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.
Gagnon-Arsenault
Isabelle
I
Département de biochimie & microbiologie and Centre de Recherche sur la fonction, la structure et l'ingéniérie des proteins, Université Laval, Québec, QC, Canada.
Tremblay
Jessy
J
Bourbonnais
Yves
Y
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D002473:Cell Wall / Q000737:chemistry; D004792:Enzyme Precursors / Q000378:metabolism; D005658:Fungi / Q000201:enzymology*; D008969:Molecular Sequence Data; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*
D004792:Enzyme Precursors; D029701:Saccharomyces cerevisiae Proteins; D016282:Aspartic Acid Endopeptidases; C119515:YPS3 protein, S cerevisiae; C499266:YPS1 protein, S cerevisiae