BAIT

SLM1

LIT2, YIL105C
Phosphoinositide PI4,5P(2) binding protein, forms a complex with Slm2p; acts downstream of Mss4p in a pathway regulating actin cytoskeleton organization in response to stress; phosphorylated by the TORC2 complex; protein abundance increases in response to DNA replication stress; SLM1 has a paralog, SLM2, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

CMP2

CNA2, calcineurin catalytic subunit A, L000000368, YML057W
Calcineurin A; one isoform (the other is Cna1p) of the catalytic subunit of calcineurin, a Ca++/calmodulin-regulated protein phosphatase which regulates Crz1p (a stress-response transcription factor), the other calcineurin subunit is CNB1; regulates the function of Aly1p alpha-arrestin; CMP2 has a paralog, CNA1, that arose from the whole genome duplication
Kinome Project (Sc)
GO Process (2)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

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.

Publication

The phosphatidylinositol 4,5-biphosphate and TORC2 binding proteins Slm1 and Slm2 function in sphingolipid regulation.

Tabuchi M, Audhya A, Parsons AB, Boone C, Emr SD

The Stt4 phosphatidylinositol 4-kinase has been shown to generate a pool of phosphatidylinositol 4-phosphate (PI4P) at the plasma membrane, critical for actin cytoskeleton organization and cell viability. To further understand the essential role of Stt4-mediated PI4P production, we performed a genetic screen using the stt4(ts) mutation to identify candidate regulators and effectors of PI4P. From this analysis, we identified several ... [more]

Mol. Cell. Biol. Aug. 01, 2006; 26(15);5861-75 [Pubmed: 16847337]

Throughput

  • Low Throughput

Curated By

  • BioGRID