Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Molecular microbiology - 1 Aug 2008

Gagnon-Arsenault Isabelle, Parisé Luc, Tremblay Jessy, Bourbonnais Yves

Abstract excerpt

Yeast 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 alpha/beta two-subunit enzyme. Here we...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Arginine
Share to Aspartic Acid Endopeptidases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Catalysis

Share to Cell Wall

Share to Enzyme Activation

Share to Glycosylphosphatidylinositols

Share to Hydrogen-Ion Concentration

Share to Proprotein Convertases

Source

Identifiers

PMID: 18573178
DOI: 10.1111/j.1365-2958.2008.06339.x

Genes

GPI

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Activation mechanism, functional role and shedding of glycosylphosphatidylinositol-anchored Yps1p at the Saccharomyces cerevisiae cell surface.PMID 18573178Read ↗

Absence of Yps7p, a putative glycosylphosphatidylinositol-linked aspartyl protease in Pichia pastoris, results in aberrant cell wall composition and increased osmotic stress resistance.Semantic proximity Read ↗

Glycosylphosphatidylinositol-anchored proteases of Candida albicans target proteins necessary for both cellular processes and host-pathogen interactions.Semantic proximity Read ↗

A novel role for a glycosylphosphatidylinositol-anchored aspartyl protease, CgYps1, in the regulation of pH homeostasis in Candida glabrata.Semantic proximity Read ↗

Generating anchors only to lose them: The unusual story of glycosylphosphatidylinositol anchor biosynthesis and remodeling in yeast and fungi.Semantic proximity Read ↗

Proteolytic function of GPI-anchored plasma membrane protease Yps1p in the yeast vacuole and Golgi.Semantic proximity Read ↗

A family of glycosylphosphatidylinositol-linked aspartyl proteases is required for virulence of Candida glabrata.Semantic proximity Read ↗

Proteolytic processing of the Saccharomyces cerevisiae cell wall protein Scw4 regulates its activity and influences its covalent binding to glucan.Semantic proximity Read ↗

Involvement of cell surface glycosyl-phosphatidylinositol-linked aspartyl proteases in alpha-secretase-type cleavage and ectodomain solubilization of human Alzheimer beta-amyloid precursor protein in yeast.Semantic proximity Read ↗

GUP1 of Saccharomyces cerevisiae encodes an O-acyltransferase involved in remodeling of the GPI anchor.Semantic proximity Read ↗

Ssy5 is a signaling serine protease that exhibits atypical biogenesis and marked S1 specificity.Semantic proximity Read ↗

Active site determination of Gpi8p, a caspase-related enzyme required for glycosylphosphatidylinositol anchor addition to proteins.Semantic proximity Read ↗

The glycosylphosphatidylinositol-linked aspartyl protease Yps1 is transcriptionally regulated by the calcineurin-Crz1 and Slt2 MAPK pathways in Candida glabrata.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.