The BioGRID | PUBLICATION VIEW

	FEBS Lett. Nov (2003); 554(1):10-6
The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance.
Fuchs U, Rehkamp GF, Slany R, Follo M, Borkhardt A
Children's University Hospital, Department of Hematology and Oncology, Feulgenstrasse 12, 35392 Giessen, Germany. uta.e.fuchs@paediat.med.uni-giessen.de
Abstract: In acute myelogenous and lymphoid leukemias, rearrangements involving the MLL (mixed lineage leukemia) gene at chromosome 11q23 are frequent. The truncated MLL protein is fused in-frame to a series of partner proteins. We previously identified the formin-binding protein 17 (FBP17) as such an MLL fusion partner. In this study, we explored in vivo physiological interaction partners of FBP17 using a two-hybrid assay and found tankyrase (TNKS), an ADP-ribose polymerase protein involved in telomere maintenance and mitogen-activated protein kinase signaling. We demonstrate that FBP17 binds via a special TNKS-binding motif to tankyrase. The physiological relevance is indicated by co-immunoprecipitation of endogenous proteins in 293T cells.
[PUBMED: 14596906]