BAIT

SAC1

RSD1, phosphatidylinositol-3-phosphatase SAC1, L000001790, YKL212W
Phosphatidylinositol phosphate (PtdInsP) phosphatase; involved in hydrolysis of PtdIns[4]P in the early and medial Golgi; regulated by interaction with Vps74p; ER localized transmembrane protein which cycles through the Golgi; involved in protein trafficking and processing, secretion, and cell wall maintenance; regulates sphingolipid biosynthesis through the modulation of PtdIns(4)P metabolism
Saccharomyces cerevisiae (S288c)
PREY

PMT2

FUN25, dolichyl-phosphate-mannose-protein mannosyltransferase PMT2, L000000642, L000001459, YAL023C
Protein O-mannosyltransferase of the ER membrane; transfers mannose residues from dolichyl phosphate-D-mannose to protein serine/threonine residues; involved in ER quality control; acts in a complex with Pmt1p, can instead interact with Pmt5p; antifungal drug target; PMT2 has a paralog, PMT3, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)

Affinity Capture-MS

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 is identified by mass spectrometric methods.

Publication

ER-to-plasma membrane tethering proteins regulate cell signaling and ER morphology.

Manford AG, Stefan CJ, Yuan HL, Macgurn JA, Emr SD

Endoplasmic reticulum-plasma membrane (ER-PM) junctions are conserved structures defined as regions of the ER that tightly associate with the plasma membrane. However, little is known about the mechanisms that tether these organelles together and why such connections are maintained. Using a quantitative proteomic approach, we identified three families of ER-PM tethering proteins in yeast: Ist2 (related to mammalian TMEM16 ion ... [more]

Dev. Cell Dec. 11, 2012; 23(6);1129-40 [Pubmed: 23237950]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
PMT2 SAC1
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.3638BioGRID
2075882

Curated By

  • BioGRID