ArticleProceedings of the National Academy of Sciences of the United States of America1995
Shared functions in vivo of a glycosyl-phosphatidylinositol-linked aspartyl protease, Mkc7, and the proprotein processing protease Kex2 in yeast.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 96 citations in OpenAlex.
- FvKex2 is required for development, virulence, and mycotoxin production in Fusarium verticillioides.Applied microbiology and biotechnology · 2024Article
- Global analysis of Saccharomyces cerevisiae growth in mucin.G3 (Bethesda, Md.) · 2021Article
- Systematic Comparison of Cell Wall-Related Proteins of Different Yeasts.Journal of fungi (Basel, Switzerland) · 2021Article
- Evolutionary Overview of Molecular Interactions and Enzymatic Activities in the Yeast Cell Walls.International journal of molecular sciences · 2020Review
- Tracking yeast pheromone receptor Ste2 endocytosis using fluorogen-activating protein tagging.Molecular biology of the cell · 2018Article
- The Vps13p-Cdc31p complex is directly required for TGN late endosome transport and TGN homotypic fusion.The Journal of cell biology · 2017Article
- Role of the unfolded protein response in regulating the mucin-dependent filamentous-growth mitogen-activated protein kinase pathway.Molecular and cellular biology · 2015Article
- Kexin-like endoprotease KexB is required for N-glycan processing, morphogenesis and virulence in Aspergillus fumigatus.Fungal genetics and biology : FG & B · 2015Article
- Direct binding of the Kex2p cytosolic tail to the VHS domain of yeast Gga2p facilitates TGN to prevacuolar compartment transport and is regulated by phosphorylation.Molecular biology of the cell · 2013Article
- The Golgi-resident protease Kex2 acts in conjunction with Prm1 to facilitate cell fusion during yeast mating.The Journal of cell biology · 2007Article
- Yapsins are a family of aspartyl proteases required for cell wall integrity in Saccharomyces cerevisiae.Eukaryotic cell · 2005Article
- Reduced proteolysis of secreted gelatin and Yps1-mediated alpha-factor leader processing in a Pichia pastoris kex2 disruptant.Applied and environmental microbiology · 2005Article
- Disordered cell integrity signaling caused by disruption of the kexB gene in Aspergillus oryzae.Eukaryotic cell · 2004Article
- Mutations that are synthetically lethal with a gas1Delta allele cause defects in the cell wall of Saccharomyces cerevisiae.Molecular genetics and genomics : MGG · 2003Article
- Yeast genes controlling responses to topogenic signals in a model transmembrane protein.Molecular biology of the cell · 2002Article
- Advances in the cellular and molecular biology of the beta-amyloid protein in Alzheimer's disease.Neuromolecular medicine · 2002Review
- Tagging morphogenetic genes by insertional mutagenesis in the yeast Yarrowia lipolytica.Journal of bacteriology · 2001Article
- Characterization of the kexin-like maturase of Aspergillus niger.Applied and environmental microbiology · 2000Article
- Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins.Journal of bacteriology · 1999Article
- Identification and characterization of Saccharomyces cerevisiae yapsin 3, a new member of the yapsin family of aspartic proteases encoded by the YPS3 gene.The Biochemical journal · 1999Article
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2 authors at 1 institution in 1 country.
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Abstract
The MKC7 gene was isolated as a multicopy suppressor of the cold-sensitive growth phenotype of a yeast kex2 mutant, which lacks the protease that cleaves pro-alpha-factor and other secretory proproteins at pairs of basic residues in a late Golgi compartment in yeast. MKC7 encodes an aspartyl protease most closely related to product of the YAP3 gene, a previously isolated multicopy suppressor of the pro-alpha-factor processing defect of a kex2 null. Multicopy MKC7 suppressed the alpha-specific mating defect of a kex2 null as well as multicopy YAP3 did, but multicopy YAP3 was a relatively weak suppressor of kex2 cold sensitivity. Overexpression of MKC7 resulted in production of a membrane-associated proteolytic activity that cleaved an internally quenched fluorogenic peptide substrate on the carboxyl side of a Lys-Arg site. Treatment with phosphatidylinositol-specific phospholipase C shifted Mkc7 activity from the detergent to the aqueous phase in a Triton X-114 phase separation, indicating that membrane attachment of Mkc7 is mediated by a glycosyl-phosphatidylinositol anchor. Although disruption of MKC7 or YAP3 alone resulted in no observable phenotype, mkc7 yap3 double disruptants exhibited impaired growth at 37 degrees C. Disruption of MKC7 and YAP3 in a kex2 null mutant resulted in profound temperature sensitivity and more generalized cold sensitivity. The synergism of mkc7, yap3, and kex2 null mutations argues that Mkc7 and Yap3 are authentic processing enzymes whose functions overlap those of Kex2 in vivo.
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