Interaction between NBS1 and the mTOR/Rictor/SIN1 complex through specific domains.
Where this comes from
- Record sourced from PubMed, PMID 23762398.
- Also identified by DOI 10.1371/journal.pone.0065586 and PMC identifier 3675082.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
Abstract
Nijmegen breakage syndrome (NBS) is a chromosomal-instability syndrome. The NBS gene product, NBS1 (p95 or nibrin), is a part of the Mre11-Rad50-NBS1 complex. SIN1 is a component of the mTOR/Rictor/SIN1 complex mediating the activation of Akt. Here we show that NBS1 interacted with mTOR, Rictor, and SIN1. The specific domains of mTOR, Rictor, or SIN1 interacted with the internal domain (a.a. 221-402) of NBS1. Sucrose density gradient showed that NBS1 was located in the same fractions as the mTOR/Rictor/SIN1 complex. Knockdown of NBS1 decreased the levels of phosphorylated Akt and its downstream targets. Ionizing radiation (IR) increased the NBS1 levels and activated Akt activity. These results demonstrate that NBS1 interacts with the mTOR/Rictor/SIN1 complex through the a.a. 221-402 domain and contributes to the activation of Akt activity.
Medical subject headings
- Adaptor Proteins, Signal Transducing
- Carrier Proteins
- Cell Cycle Proteins
- Nuclear Proteins
- Proto-Oncogene Proteins c-akt
- Signal Transduction
- TOR Serine-Threonine Kinases