Interaction of RAFT1 with gephyrin required for rapamycin-sensitive signaling

David M. Sabatini, Roxanne K. Barrow, Seth Blackshaw, Patrick E. Burnett, Michael M. Lai, Michael E. Field, Ben A. Bahr, Joachim Kirsch, Heinrich Betz, Solomon H. Snyder

Research output: Contribution to journalArticlepeer-review

149 Scopus citations


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 56 kinase and the elF-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.

Original languageEnglish (US)
Pages (from-to)1161-1164
Number of pages4
Issue number5417
StatePublished - May 14 1999

ASJC Scopus subject areas

  • General


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