Gene interactions and pathways from curated databases and text-mining
Science 1999, PMID: 10325225

Interaction of RAFT1 with gephyrin required for rapamycin-sensitive signaling.

Sabatini, D M; Barrow, R K; Blackshaw, S; Burnett, P E; Lai, M M; Field, M E; Bahr, B A; Kirsch, J; Betz, H; Snyder, S H

RAFT1 (rapamycin and FKBP12 target 1; also called FRAP or mTOR) is a member of the ATM (ataxia telangiectasia mutated)-related family of proteins and functions as the in vivo mediator of the effects of the immunosuppressant rapamycin and as an important regulator of messenger RNA translation. In mammalian cells RAFT1 interacted with gephyrin, a widely expressed protein necessary for the clustering of glycine receptors at the cell membrane of neurons. RAFT1 mutants that could not associate with gephyrin failed to signal to downstream molecules, including the p70 ribosomal S6 kinase and the eIF-4E binding protein, 4E-BP1. The interaction with gephyrin ascribes a function to the large amino-terminal region of an ATM-related protein and reveals a role in signal transduction for the clustering protein gephyrin.

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Text Mining Data

Dashed line = No text mining data

Manually curated Databases

  • IRef Biogrid Interaction: GPHN — MTOR (physical association, affinity chromatography technology)
  • IRef Biogrid Interaction: GPHN — MTOR (direct interaction, pull down)
  • IRef Hprd Interaction: GPHN — MTOR (in vivo)
  • IRef Hprd Interaction: GPHN — MTOR (in vitro)
  • IRef Hprd Interaction: GPHN — MTOR (two hybrid)
  • IRef Innatedb Interaction: GPHN — MTOR (unknown, -)
In total, 1 gene pairs are associated to this article in curated databases