Ptk2 contributes to osmoadaptation in the filamentous fungus Neurospora crassa

Fungal Genet Biol. 2009 Dec;46(12):949-55. doi: 10.1016/j.fgb.2009.09.005. Epub 2009 Sep 20.

Abstract

Hyphal tip-growing organisms often rely upon an internal hydrostatic pressure (turgor) to drive localized expansion of the cell. Regulation of the turgor in response to osmotic shock is mediated primarily by an osmotic MAP kinase cascade which activates osmolyte synthesis and ion uptake to effect turgor recovery. We characterized a Neurospora crassa homolog (PTK2) of ser/thr kinase regulators of ion transport in yeast to determine its role in turgor regulation in a filamentous fungi. The ptk2 mutant is osmosensitive, and has lower turgor poise than wildtype. The cause appears to be lower activity of the plasma membrane H+-ATPase. Its role in osmoadaptation is unrelated to the activity of the osmotic MAP kinase cascade. Instead, it acts in an alternative pathway that, like the osmotic MAP kinase cascade, also involves ion transport mediated osmoadaptation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptation, Physiological*
  • Cell Membrane Permeability
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Homeostasis
  • Hydrostatic Pressure
  • Hyphae / growth & development
  • Ion Transport
  • MAP Kinase Signaling System
  • Membrane Potentials
  • Mutation
  • Neurospora crassa / enzymology
  • Neurospora crassa / genetics
  • Neurospora crassa / physiology*
  • Osmolar Concentration
  • Osmotic Pressure
  • Patch-Clamp Techniques
  • Protein-Serine-Threonine Kinases / genetics
  • Protein-Serine-Threonine Kinases / metabolism*
  • Proton-Translocating ATPases / genetics
  • Proton-Translocating ATPases / metabolism
  • Saccharomyces cerevisiae / physiology

Substances

  • Fungal Proteins
  • Protein-Serine-Threonine Kinases
  • Proton-Translocating ATPases