title: Stress-regulated kinase pathways in the recovery of tip growth and microtubule dynamics following osmotic stress in S. pombe.
abstract: The cell-integrity and stress-response MAP kinase pathways (CIP and SRP, respectively) are stimulated by various environmental stresses. Ssp1 kinase modulates actin dynamics and is rapidly recruited to the plasma membrane following osmotic stress. Here, we show that osmotic stress arrested tip growth, induced the deposition of abnormal cell-wall deposits at tips and led to disassociation of F-actin foci from cell tips together with a reduction in the amount of F-actin in these foci. Osmotic stress also ;froze' the dynamics of interphase microtubule bundles, with microtubules remaining static for approximately 38 minutes (at 30 degrees C) before fragmenting upon return to dynamic behaviour. The timing with which microtubules resumed dynamic behaviour relied upon SRP activation of Atf1-mediated transcription, but not on either CIP or Ssp1 signalling. Analysis of the recovery of tip growth showed that: (1) the timing of recovery was controlled by SRP-stimulated Atf1 transcription; (2) re-establishment of polarized tip growth was absolutely dependent upon SRP and partially dependent upon Ssp1 signalling; and (3) selection of the site for polarized tip extension required Ssp1 and the SRP-associated polarity factor Wsh3 (also known as Tea4). CIP signalling did not impact upon any aspect of recovery. The normal kinetics of tip growth following osmotic stress of plo1.S402A/E mutants established that SRP control over the resumption of tip growth after osmotic stress is distinct from its control of tip growth following heat or gravitational stresses.
authors.affiliation: CRUK Cell Division Laboratory, Paterson Institute for Cancer Research, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK.
authors.forename: Alasdair M
authors.initials: AM
authors.lastname: Robertson
authors.forename: Iain M
authors.initials: IM
authors.lastname: Hagan
mesh_terms: D000199:Actins / Q000378:metabolism; D051697:Activating Transcription Factor 1 / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D008870:Microtubules / Q000502:physiology*; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism*; D009997:Osmotic Pressure / Q000502:physiology; D010750:Phosphoproteins / Q000378:metabolism; D012568:Schizosaccharomyces / Q000201:enzymology* / Q000254:growth & development* / Q000648:ultrastructure; D029702:Schizosaccharomyces pombe Proteins / Q000378:metabolism
chemical_list: D000199:Actins; D051697:Activating Transcription Factor 1; D018840:HSP70 Heat-Shock Proteins; D008869:Microtubule-Associated Proteins; C111935:PSS1 protein, S pombe; D010750:Phosphoproteins; D029702:Schizosaccharomyces pombe Proteins; C501888:Tea4 protein, S pombe; C106740:atf1 protein, S pombe; D020928:Mitogen-Activated Protein Kinases; C095409:sty1 protein, S pombe