Phosphorylation and binding partner analysis of the TSC1-TSC2 complex.

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Citation

Nellist M, Burgers PC, van den Ouweland AM, Halley DJ, Luider TM

Phosphorylation and binding partner analysis of the TSC1-TSC2 complex.

Biochem Biophys Res Commun. 2005 Aug 5;333(3):818-26.

PubMed ID
15963462 [ View in PubMed
]
Abstract

Tuberous sclerosis complex (TSC) is an autosomal dominant benign tumour syndrome caused by mutations to either the TSC1 or TSC2 tumour suppressor gene. The TSC1 and TSC2 gene products, TSC1 and TSC2, form a protein complex that integrates inputs from multiple signalling cascades to inactivate the small GTPase rheb, and thereby inhibit mTOR-dependent cell growth. We have used matrix-assisted laser desorption/ionisation time-of-flight and Fourier transform mass spectrometry to identify TSC1 and TSC2 phosphorylation sites and candidate TSC1 and TSC2 interacting proteins. We identified three sites of TSC2 phosphorylation and a novel site of TSC1 phosphorylation, and investigated the roles of these sites in regulating the activity of the TSC1-TSC2 complex. In addition, we identified three TSC1-TSC2 interacting proteins, including DOCK7 a putative rhebGEF.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Heat shock cognate 71 kDa proteinP11142Details