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A more recent version of this article appeared on November 12, 2004
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M409014200v1
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Papers In Press, published online ahead of print September 1, 2004
J. Biol. Chem, 10.1074/jbc.M409014200
Submitted on August 6, 2004
Revised on September 1, 2004
Accepted on September 1, 2004

AMPK-regulated phosphorylation and acetylation of importin a1: Involvement in the nuclear import of RNA-binding protein HuR

Wengong Wang, Xiaoling Yang, Tomoko Kawai, Isabel Lopez de Silanes, Krystyna Mazan-Mamczarz, Peili Chen, Yuh Min Chook, Christina Quensel, Matthias Kohler, and Myriam Gorospe

Box 12, LCMB, NIA, National Institutes of Health, Baltimore, Maryland 21228

Corresponding Author: myriam-gorospe{at}nih.gov

Nuclear import of HuR, a shuttling RNA-binding protein, is associated with reduced stability of HuR’s target mRNAs. Increased function of the AMP-activated protein kinase (AMPK), an enzyme involved in responding to metabolic stress, was recently shown to reduce the cytoplasmic levels of HuR. Here, we provide evidence that importin a1, an adaptor protein involved in nuclear import, contributes to the nuclear import of HuR through two AMPK-modulated mechanisms. First, AMPK triggered the acetylation of importin a1 on Lys-22, a process dependent on the acetylase activity of p300. Second, AMPK phosphorylated importin a1 on Ser-105. Accordingly, expression of importin a1 proteins bearing Lys-22-Arg or Ser-105-Ala mutations failed to mediate the nuclear import of HuR in intact cells. Our results point to importin a1 as a critical downstream target of AMPK and key mediator of AMPK-triggered HuR nuclear import.


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