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

Journal of Biochemistry
Shigeki ChibaShunnosuke Abe

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 a 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 Ser(245) residue (Ser(246) in human) and that these proteins are associated at the plasma membrane. Ser(245) was also found to be a substrate for AKT and the resulting Ser(245) 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 Ser(245) is the principal target for the modulation of this protein via the AKT signalling cascade.

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Citations

Jan 1, 2013·Molecules and Cells·Young-Mi Kim, Do-Hyung Kim
Nov 17, 2010·Molecular and Cellular Biology·Sandra L ClementJens Lykke-Andersen
Sep 22, 2011·Wiley Interdisciplinary Reviews. RNA·Roberto GherziPaola Briata
May 12, 2012·Molecular Cell·Young-Mi KimDo-Hyung Kim
Mar 25, 2021·Developmental Cell·Christoph J BurckhardtGaudenz Danuser

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