ArticleMolecular and cellular biology2009
Identification of the serine 307 of LKB1 as a novel phosphorylation site essential for its nucleocytoplasmic transport and endothelial cell angiogenesis.
Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 96 citations in OpenAlex.
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- Truncated LKB1 nonenzymatically enhances Fas-induced apoptosis by acting as a surrogate of Smac.Cell death discovery · 2025Article
- LKB1 biology: assessing the therapeutic relevancy of LKB1 inhibitors.Cell communication and signaling : CCS · 2024Review
- The LKB1-TSSK1B axis controls YAP phosphorylation to regulate the Hippo-YAP pathway.Cell death & disease · 2024Article
- Spatial regulation of AMPK signaling revealed by a sensitive kinase activity reporter.Nature communications · 2022Article
- The Inositol Phosphate System-A Coordinator of Metabolic Adaptability.International journal of molecular sciences · 2022Review
- Alzheimer risk gene product Pyk2 suppresses tau phosphorylation and phenotypic effects of tauopathy.Molecular neurodegeneration · 2022Article
- Folliculin haploinsufficiency causes cellular dysfunction of pleural mesothelial cells.Scientific reports · 2021Article
- Autophagic degradation of KAT2A/GCN5 promotes directional migration of vascular smooth muscle cells by reducing TUBA/α-tubulin acetylation.Autophagy · 2020Article
- The Key Role of IPMolecules (Basel, Switzerland) · 2020Review
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- The natural product antroalbol H promotes phosphorylation of liver kinase B1 (LKB1) at threonine 189 and thereby enhances cellular glucose uptake.The Journal of biological chemistry · 2019Article
- Metformin and glucose starvation decrease the migratory ability of hepatocellular carcinoma cells: targeting AMPK activation to control migration.Scientific reports · 2019Article
- PKA Activates AMPK Through LKB1 Signaling in Follicular Thyroid Cancer.Frontiers in endocrinology · 2019Article
- Metformin Inhibits the NLRP3 Inflammasome via AMPK/mTOR-dependent Effects in Diabetic Cardiomyopathy.International journal of biological sciences · 2019Article
- l-Alanine activates hepatic AMP-activated protein kinase and modulates systemic glucose metabolism.Molecular metabolism · 2018Article
- Upregulation of liver kinase B1 predicts poor prognosis in hepatocellular carcinoma.International journal of oncology · 2018Article
- AMPK Function in Mammalian Spermatozoa.International journal of molecular sciences · 2018Review
3 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
Abstract
LKB1, a master kinase that controls at least 13 downstream protein kinases including the AMP-activated protein kinase (AMPK), resides mainly in the nucleus. A key step in LKB1 activation is its export from the nucleus to the cytoplasm. Here, we identified S307 of LKB1 as a putative novel phosphorylation site which is essential for its nucleocytoplasmic transport. In a cell-free system, recombinant PKC-zeta phosphorylates LKB1 at S307. AMPK-activating agents stimulate PKC-zeta activity and LKB1 phosphorylation at S307 in endothelial cells, hepatocytes, skeletal muscle cells, and vascular smooth muscle cells. Like the kinase-dead LKB1 D194A mutant (mutation of Asp194 to Ala), the constitutively nucleus-localized LKB1 SL26 mutant and the LKB1 S307A mutant (Ser307 to Ala) exhibit a decreased association with STRAD alpha. Interestingly, the PKC-zeta consensus sequence surrounding LKB1 S307 is disrupted in the LKB1 SL26 mutant, thus providing a likely molecular explanation for this mutation causing LKB1 dysfunction. In addition, LKB1 nucleocytoplasmic transport and AMPK activation in response to peroxynitrite are markedly reduced by pharmacological inhibition of CRM1, which normally facilitates nuclear export of LKB1-STRAD complexes. In comparison to the LKB1 wild type, the S307A mutant complexes show reduced association with CRM1. Finally, adenoviral overexpression of wild-type LKB1 suppresses, while the LKB1 S307A mutant increases, tube formation and hydrogen peroxide-enhanced apoptosis in cultured endothelial cells. Taken together, our results suggest that, in multiple cell types the signaling pathways engaged by several physiological stimuli converge upon PKC-zeta-dependent LKB1 phosphorylation at S307, which directs the nucleocytoplasmic transport of LKB1 and consequent AMPK activation.
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