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J. Biol. Chem., Vol. 277, Issue 51, 49101-49104, December 20, 2002
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From the The p75 neurotrophin receptor has been implicated
in diverse aspects of neurotrophin signaling, but the mechanisms by
which its effects are mediated are not well understood. Here we
identify two MAGE proteins, necdin and MAGE-H1, as interactors for the intracellular domain of p75 and show that the interaction is enhanced by ligand stimulation. PC12 cells transfected with necdin or MAGE-H1 exhibit accelerated differentiation in response to nerve growth factor. Expression of these two MAGE proteins is predominantly cytoplasmic in PC12 cells, and necdin was found to be capable of
homodimerization, suggesting that it may act as a cytoplasmic adaptor
to recruit a signaling complex to p75. These findings indicate that
diverse MAGE family members can interact with the p75 receptor and
highlight type II MAGE proteins as a potential family of interactors
for signaling proteins containing type II death domains.
Molecular Neurobiology Group, Department of
Biological Chemistry, Weizmann Institute of Science, 76100 Rehovot,
Israel, the § Division of Regulation of Macromolecular
Functions, Institute for Protein Research, Osaka University, Osaka
565-0871, Japan, and the ¶ Department of Medical
Biochemistry and Biophysics, Karolinska Institute, S-17177
Stockholm, Sweden
Incumbent of the Daniel Koshland Sr. Career Development Chair
at the Weizmann Institute of Science. To whom correspondence should be
addressed. Tel.: 972-8-934-4266; Fax: 972-8-934-4112; E-mail:
mike.fainzilber@weizmann.ac.il.
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