4.6 Article

The Hog1 Stress-activated Protein Kinase Targets Nucleoporins to Control mRNA Export upon Stress

Journal

JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 288, Issue 24, Pages 17384-17398

Publisher

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.444042

Keywords

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Funding

  1. MINECO (Spanish government) [BFU2012-33503]
  2. Consolider Ingenio program [CSD2007-0015]
  3. Fundacion Marcelino Botin [BFU2011-26722]
  4. MINECO [BFU2011-23418]
  5. Agence Nationale de la Recherche (Nucleopol and ODynRib-Jeune chercheur program)
  6. Jeune equipe from Fondation pour la Recherche Medicale
  7. ICREA Academia (Generalitat de Catalunya)

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The control of mRNA biogenesis is exerted at several steps. In response to extracellular stimuli, stress-activated protein kinases (SAPK) modulate gene expression to maximize cell survival. In yeast, the Hog1 SAPK plays a key role in reprogramming the gene expression pattern required for cell survival upon osmostress by acting during transcriptional initiation and elongation. Here, we genetically show that an intact nuclear pore complex is important for cell survival and maximal expression of stress-responsive genes. The Hog1 SAPK associates with nuclear pore complex components and directly phosphorylates the Nup1, Nup2, and Nup60 components of the inner nuclear basket. Mutation of those factors resulted in a deficient export of stress-responsive genes upon stress. Association of Nup1, Nup2, and Nup60 to stress-responsive promoters occurs upon stress depending on Hog1 activity. Accordingly, STL1 gene territory is maintained at the nuclear periphery upon osmostress in a Hog1-dependent manner. Cells containing non-phosphorylatable mutants in Nup1 or Nup2 display reduced expression of stress-responsive genes. Together, proper mRNA biogenesis of stress-responsive genes requires of the coordinate action of synthesis and export machineries by the Hog1 SAPK.

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