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Liver‐type fatty acid binding protein interacts with hepatocyte nuclear factor 4α
Author(s) -
McIntosh Avery L.,
Petrescu Anca D.,
Hostetler Heather A.,
Kier Ann B.,
Schroeder Friedhelm
Publication year - 2013
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/j.febslet.2013.09.043
Subject(s) - hepatocyte nuclear factor 4 , förster resonance energy transfer , transactivation , chemistry , fatty acid binding protein , hepatocyte nuclear factors , microbiology and biotechnology , biophysics , biochemistry , biology , fluorescence , gene expression , gene , transcription factor , nuclear receptor , physics , quantum mechanics
Hepatocyte nuclear factor 4α (HNF4α) regulates liver type fatty acid binding protein (L‐FABP) gene expression. Conversely as shown herein, L‐FABP structurally and functionally also interacts with HNF4α. Fluorescence resonance energy transfer (FRET) between Cy3‐HNF4α (donor) and Cy5‐L‐FABP (acceptor) as well as FRET microscopy detected L‐FABP in close proximity (∼80 Å) to HNF4α, binding with high affinity K d ∼250–300 nM. Circular dichroism (CD) determined that the HNF4α/L‐FABP interaction altered protein secondary structure. Finally, L‐FABP potentiated transactivation of HNF4α in COS7 cells. Taken together, these data suggest that L‐FABP provides a signaling path to HNF4α activation in the nucleus.