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The formin‐binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance
Author(s) -
Fuchs U.,
Rehkamp G.F.,
Slany R.,
Follo M.,
Borkhardt A.
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01063-9
Subject(s) - telomere , telomere binding protein , microbiology and biotechnology , formins , chemistry , binding protein , dna binding protein , biology , transcription factor , biochemistry , dna , gene , actin cytoskeleton , cytoskeleton , cell
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.