In Vivo Processing of Nonanchored Yapsin 1 (Yap3p)

Olsen, Vicki; Loh, Y. Peng

doi:10.1006/abbi.1999.1665

Cited by 9 publications

(12 citation statements)

References 31 publications

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“…2 highlights the important sequential processing steps leading to a fully active enzyme at the cell surface for fungal yapsins composed of two subunits. Recent experimental data (Tremblay J, Parisé L, Gagnon‐Arsenault I & Bourbonnais Y, in preparation) are in agreement with a final step requiring the activity of an aminopeptidase for maturation of the extended β subunit upon arrival of the enzyme at the cell surface, as proposed in earlier studies (Olsen & Loh, 2000).…”

Section: Zymogen Activationsupporting

confidence: 81%

“…The heterodimer resulted from endoproteolytic cleavage, probably followed by exopeptidase trimming (see below), within an internal loop also identified in many but not all fungal yapsins (see ‘Domain organization’ above). In another study in which the biosynthesis of this secreted version of Sc Yps1p was monitored by pulse‐chase labelling studies, the same group reported that the proteolytic processing step to generate the α and β subunits was an early event occurring within the ER (Olsen & Loh, 2000). Importantly, because the α and β subunits still reacted with antibodies directed, respectively, against the propeptide (Y 46 –E 61 ) or the insertion loop (S 124 –S 138 ), this initial cleavage was proposed to generate extended forms of both α and β subunits.…”

Section: Zymogen Activationmentioning

confidence: 99%

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

Gagnon‐Arsenault

Tremblay

Bourbonnais

2006

FEMS Yeast Research

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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.

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Section: Zymogen Activationsupporting

confidence: 81%

Section: Zymogen Activationmentioning

confidence: 99%

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

Gagnon‐Arsenault

Tremblay

Bourbonnais

2006

FEMS Yeast Research

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“…Unlike most aspartic peptidases, Yps1p is further subjected to an internal cleavage within a loop insertion, compared with pepsin, to generate an α/β two‐subunit endopeptidase (Cawley et al ., 1998; Olsen and Loh, 2000). In the present study, we demonstrated that this cleavage is exclusively autocatalytic for GPI‐Yps1p (Fig.…”

Section: Discussionsupporting

confidence: 69%

Activation mechanism, functional role and shedding of glycosylphosphatidylinositol‐anchored Yps1p at the Saccharomyces cerevisiae cell surface

Gagnon‐Arsenault

Parisé

Tremblay

et al. 2008

Molecular Microbiology

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SummaryYeast cell wall assembly is a highly regulated and dynamic process. A class of cell surface aspartic peptidases anchored by a glycosylphosphatidylinositol (GPI) group, collectively known as yapsins, was proposed to be involved in cell wall construction. The Saccharomyces cerevisiae Yps1p, the prototypal yapsin, is processed internally within a loop region to produce an a/b two-subunit enzyme. Here we investigated the activation mechanism of GPI-anchored Yps1p and identified some of its substrates. We report that all activation steps of GPI-Yps1p take place at the cell surface and are regulated by the environmental pH. GPI-Yps1p is active in vivo at pH 6.0 and pH 3.0 and functions as a sheddase for a subset of GPI-anchored enzymes, including itself and the Gas1 glucanosyltransferase. Importantly, while native GPI-Yps1p weakly suppresses many phenotypes associated with the yeast kex2D mutant, loop mutants that interfere with conversion into the two-subunit enzyme restore the kex2D phenotypes to near wild type level. We propose that cleavage of this internal loop region plays an important regulatory function through stimulating its shedding activity. Collectively, our data provide a direct link between the pH regulation of yeast cell wall assembly and the activity of a yapsin.

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“…The genome sequence of S. cerevisiae has revealed the presence of multiple members of the yapsin family, i.e., five YPS genes, YPS1, YPS2, YPS3, YPS6 and YPS7 (Olsen et al, 1999). As GPI-anchoring proteins, yapsins locate on the cell surface of S. cerevisiae, but can be also released from the cell by specific phospholipases (Cawley and Loh, 1998;Olsen and Loh, 2000). Therefore, it is highly likely that yapsins are responsible for degrading recombinant proteins secreted extracellularly.…”

Section: Discussionmentioning

confidence: 98%

Multiple-yapsin-deficient mutant strains for high-level production of intact recombinant proteins in Saccharomyces cerevisiae

Cho

Cheon

Kim

et al. 2010

Journal of Biotechnology

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In Vivo Processing of Nonanchored Yapsin 1 (Yap3p)

Cited by 9 publications

References 31 publications

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

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

Activation mechanism, functional role and shedding of glycosylphosphatidylinositol‐anchored Yps1p at the Saccharomyces cerevisiae cell surface

Multiple-yapsin-deficient mutant strains for high-level production of intact recombinant proteins in Saccharomyces cerevisiae

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