Disease relevance of KRE1

• Here bacterial carboxylesterase EstA from Burkholderia gladioli was covalently anchored into the cell wall of Saccharomyces cerevisiae by in-frame fusion to the endogenous yeast proteins Kre1p, Cwp2p, and Flo1p [1].

High impact information on KRE1

• Kre1p, the plasma membrane receptor for the yeast K1 viral toxin [2].
• Toxin binding to spheroplasts is mediated by Kre1p, a cell wall protein initially attached to the plasma membrane by its C-terminal GPI anchor [2].
• Gene disruption of the KRE1 locus leads to a 40% reduced level of cell wall (1----6)-beta-glucan [3].
• The Saccharomyces cerevisiae KRE1 gene encodes a Ser/Thr-rich protein, that is directed into the yeast secretory pathway, where it is highly modified, probably through addition of O-linked mannose residues [3].
• The strong genetic interactions of CWH41 with KRE6 and KRE1, two other genes involved in the beta-1,6-glucan biosynthetic pathway, disappear in the absence of dolichol-P-glucose synthase (alg5Delta) [4].

Biological context of KRE1

• Sequencing analysis of a 15.4 kb fragment of yeast chromosome XIV identifies the RPD3, PAS8 and KRE1 loci, five new open reading frames [5].
• Kre1p is O-glycosylated, but the basis for the majority of its post-translational modification is unknown [6].

Anatomical context of KRE1

• Indirect immunoflurorescence demonstrates that Kre1p localizes to the cell surface, where it becomes concentrated at the surface of mother cells [6].
• Expression of K28-Kre1p, an inactive C-terminal fragment of Kre1p retaining its toxin affinity and membrane anchor, fully restored toxin binding and sensitivity to spheroplasts, while intact cells remained resistant [2].

Associations of KRE1 with chemical compounds

• The KRE1 gene of Saccharomyces cerevisiae, sacKRE1, appears to be involved in the synthesis of cell wall beta-glucan [7].
• A comparison between planktonic and biofilm populations of transcript abundance for genes coding for enzymes in the ergosterol (ERG1, -3, -5, -6, -9, -11, and -25) and beta-1,6-glucan (SKN and KRE1, -5, -6, and -9) pathways was performed by quantitative RT-PCR [8].

Other interactions of KRE1

• MUQ1 and KRE1, encoding proteins associated with cell surface maintenance, were also detected [9].
• A functional, epitope-tagged Kre1p is shown to be highly modified in a SEC53-dependent manner [6].
• Such a localization of Kre1p seems to parallel the CAL1/CSD2-dependent cell wall deposition of chitin found in S. cerevisiae, and is consistent with evidence from Schizophyllum commune that (1-->6)-beta-glucan accumulates during maturation of the subapical region of the wall distal to the hyphal tip [6].
• In the case of Kre1/EstA/Flo1p, in vivo maturation within the yeast secretory pathway and final incorporation into the wall were further enhanced when there was constitutive activation of the unfolded protein response pathway [1].
• In a yeast gpi1 mutant, a green-fluorescent-protein-tagged Kre1p derivative is secreted into the medium, indicating an at least transient GPI-anchoring stage of Kre1p during its processing within the yeast secretory pathway [10].

References