BAIT

SDS22

EGP1, L000002590, YKL193C
Regulatory subunit of the type 1 protein phosphatase (PP1) Glc7p; whether it functions as a positive or negative regulator of Glc7p is controversial; involved in the regulation of Glc7p nuclear localization and function
GO Process (2)
GO Function (2)
GO Component (3)
Saccharomyces cerevisiae (S288c)
PREY

YPI1

YFR003C
Regulatory subunit of the type I protein phosphatase (PP1) Glc7p; Glc7p participates in the regulation of a variety of metabolic processes including mitosis and glycogen metabolism; in vitro evidence suggests Ypi1p is an inhibitor of Glc7p while in vivo evidence suggests it is an activator; overproduction causes decreased cellular content of glycogen; partial depletion causes lithium sensitivity, while overproduction confers lithium-tolerance
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

YPI1 and SDS22 proteins regulate the nuclear localization and function of yeast type 1 phosphatase Glc7.

Pedelini L, Marquina M, Arino J, Casamayor A, Sanz L, Bollen M, Sanz P, Garcia-Gimeno MA

We have recently characterized Ypi1 as an inhibitory subunit of yeast Glc7 PP1 protein phosphatase. In this work we demonstrate that Ypi1 forms a complex with Glc7 and Sds22, another Glc7 regulatory subunit that targets the phosphatase to substrates involved in cell cycle control. Interestingly, the combination of equimolar amounts of Ypi1 and Sds22 leads to an almost full inhibition ... [more]

J. Biol. Chem. Feb. 02, 2007; 282(5);3282-92 [Pubmed: 17142459]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
YPI1 SDS22
Affinity Capture-MS
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.

High-BioGRID
-
YPI1 SDS22
Affinity Capture-MS
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.

High-BioGRID
-
YPI1 SDS22
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-0.7905BioGRID
1931607
YPI1 SDS22
PCA
PCA

A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.

High-BioGRID
-
SDS22 YPI1
Two-hybrid
Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Low-BioGRID
-

Curated By

  • BioGRID