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Journal of Biochemistry Advance Access published online on January 2, 2009
Journal of Biochemistry, doi:10.1093/jb/mvn178
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

TTP at Ser245 phosphorylation by AKT is required for binding to 14-3-3

Shigeki Chibaa, Mie Tokuharaa, Eugene Hayato Moritaa and Shunnosuke Abea,*

aLaboratory of Molecular Cell Physiology, Faculty of Agriculture, Ehime University, 3-Tarumi, Matsuyama, Ehime, 7908566, Japan

*To whom correspondence should be addressed: Shunnosuke Abe, E-mail: mcblab{at}mcb.agr.ehime-u.ac.jp Fax: +81-89-946-9853 Tel: +81-89-946-9853

Received September 17, 2008; Accepted December 22, 2008


  Abstract

Transferrin receptor trafficking protein (TTP) is a key molecule for selective internalization of the transferrin receptor (Tf-R) through endocytic protein complexes. To identify the proteins that directly regulate TTP, we performed yeast two-hybrid analysis and identified 14-3-3, which can modulate the activation-state of target proteins. Subsequent analyses demonstrated that TTP directly binds to multiple 14-3-3 isotypes via its Ser245 residue (Ser246 in human) and that these proteins are associated with the plasma membrane. Ser245 was also found to be a novel substrate for AKT and the resulting Ser245 phosphorylation induced the TTP/14-3-3 interaction. Exposure to hydrogen peroxide rapidly enhanced this association in an ovarian cell line. These results suggest that TTP Ser245 is the principal target for the modulation of this protein via the AKT signaling cascade.

Key Words: 14-3-3, AKT, phosphorylation, interaction


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