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J Biol Chem, Vol. 273, Issue 32, 20128-20133, August 7, 1998
From the Dipartimento di Biochimica e Biotecnologie Mediche,
Università degli Studi di Napoli Federico II, via S. Pansini 5, 80131 Napoli, Italy
The neural protein Fe65 possesses three putative
protein-protein interaction domains: one WW domain and two
phosphotyrosine interaction/phosphotyrosine binding domains (PID1 and
PID2); the most C-terminal of these domains (PID2) interacts in
vivo with the Alzheimer's
The Fe65 Adaptor Protein Interacts through Its PID1 Domain
with the Transcription Factor CP2/LSF/LBP1
-amyloid precursor protein, whereas
the WW domain binds to Mena, the mammalian homolog of
Drosophila-enabled protein. By the interaction trap
procedure, we isolated a cDNA clone encoding a possible ligand of
the N-terminal PID/PTB domain of Fe65 (PID1). Sequence analysis of this
clone revealed that this ligand corresponded to the previously
identified transcription factor CP2/LSF/LBP1. Co-immunoprecipitation
experiments demonstrated that the interaction between Fe65 and
CP2/LSF/LBP1 also takes place in vivo between the native
molecules. The localization of both proteins was studied using
fractionated cellular extracts. These experiments demonstrated that the
various isoforms of CP2/LSF/LBP1 are differently distributed among
subcellular fractions. At least one isoform, derived from alternative
splicing (LSF-ID), is present outside the nucleus; Fe65 was found in
both fractions. Furthermore, transfection experiments with an HA-tagged
CP2/LSF/LBP1 cDNA demonstrated that Fe65 interacts also with the
nuclear form of CP2/LSF/LBP1. Considering that the analysis of Fe65
distribution in fractionated cell extracts demonstrated that this
protein is present both in nuclear and non-nuclear fractions, we
examined the expression of Fe65 deletion mutants in the two fractions.
This analysis allowed us to observe that a small region N-terminal to
the WW domain is phosphorylated and is necessary for the presence of
Fe65 in the nuclear fraction.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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