The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance.
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.
Children's University Hospital, Department of Hematology and Oncology, Feulgenstrasse 12, 35392 Giessen, Germany. uta.e.fuchs@paediat.med.uni-giessen.de
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Fuchs
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Rehkamp
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Slany
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Follo
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Borkhardt
D020816:Amino Acid Motifs; D001665:Binding Sites; D002460:Cell Line; D003593:Cytoplasm / Q000737:chemistry; D006801:Humans; D016297:Mutagenesis, Site-Directed; D011233:Precipitin Tests; D011485:Protein Binding; D017384:Sequence Deletion; D038501:Tankyrases / Q000378:metabolism* / Q000502:physiology; D016615:Telomere / Q000378:metabolism; D020798:Two-Hybrid System Techniques
D038501:Tankyrases; C418109:TNKS protein, human