BAIT

SLT2

BYC2, LYT2, MPK1, SLK2, mitogen-activated serine/threonine-protein kinase SLT2, L000001919, YHR030C
Serine/threonine MAP kinase; involved in regulating maintenance of cell wall integrity, cell cycle progression, and nuclear mRNA retention in heat shock; required for mitophagy and pexophagy; affects recruitment of mitochondria to phagophore assembly site (PAS); plays a role in adaptive response of cells to cold; regulated by the PKC1-mediated signaling pathway; SLT2 has a paralog, KDX1, that arose from the whole genome duplication
Kinome Project (Sc)
Saccharomyces cerevisiae (S288c)
PREY

SSE1

LPG3, MSI3, adenyl-nucleotide exchange factor SSE1, L000002078, YPL106C
ATPase component of heat shock protein Hsp90 chaperone complex; plays a role in determining prion variants; binds unfolded proteins; member of the heat shock protein 70 (HSP70) family; localized to the cytoplasm; deletion results in spindle elongation in S phase; SSE1 has a paralog, SSE2, that arose from the whole genome duplication
GO Process (2)
GO Function (3)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Publication

The Hsp110 protein chaperone Sse1 is required for yeast cell wall integrity and morphogenesis.

Shaner L, Gibney PA, Morano KA

Molecular chaperones direct refolding and triage decisions and support signal transduction responses to cytotoxic stress. The eukaryotic chaperone Hsp110 is represented by the SSE1/2 genes in Saccharomyces cerevisiae, which act as nucleotide exchange factors (NEFs) for cognate cytosolic Hsp70 chaperones. In this report, we present evidence that Sse1 is required for signaling through the cell integrity pathway via partnership with ... [more]

Curr. Genet. Jul. 01, 2008; 54(1);1-11 [Pubmed: 18478233]

Throughput

  • Low Throughput

Curated By

  • BioGRID