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Full-Text Articles in Life Sciences
Identification Of A Nuclear Export Signal In The Catalytic Subunit Of Amp-Activated Protein Kinase, N. Kazgan, Tyisha Williams, L. J. Forsberg, J. E. Brenman
Identification Of A Nuclear Export Signal In The Catalytic Subunit Of Amp-Activated Protein Kinase, N. Kazgan, Tyisha Williams, L. J. Forsberg, J. E. Brenman
Biology Faculty Research
The metabolic regulator AMP-activated protein kinase (AMPK) maintains cellular homeostasis through regulation of proteins involved in energy-producing and -consuming pathways. Although AMPK phosphorylation targets include cytoplasmic and nuclear proteins, the precise mechanisms that regulate AMPK localization, and thus its access to these substrates, are unclear. We identify highly conserved carboxy-terminal hydrophobic amino acids that function as a leptomycin B–sensitive, CRM1-dependent nuclear export sequence (NES) in the AMPK catalytic subunit (AMPKα). When this sequence is modified AMPKα shows increased nuclear localization via a Ran-dependent import pathway. Cytoplasmic localization can be restored by substituting well-defined snurportin-1 or protein kinase A inhibitor (PKIA) …