Reorganization of cytoskeleton in response to extracellular stimuli

2016 Fiscal Year Final Research Report

• Project Area: Plant cell wall as information-processing system
• Project/Area Number: 24114004
• Research Category: Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area)
• Allocation Type: Single-year Grants
• Review Section: Biological Sciences
• Research Institution: Nara Institute of Science and Technology
• Principal Investigator: Hashimoto Takashi 奈良先端科学技術大学院大学, バイオサイエンス研究科, 教授 (80180826)
• Co-Investigator(Renkei-kenkyūsha): KATO Takehide 奈良先端科学技術大学院大学, バイオサイエンス研究科, 助教 (70379535)
• Project Period (FY): 2012-06-28 – 2017-03-31
• Keywords: 微小管 / 環境ストレス / チューブリン / リン酸化 / 植物

Outline of Final Research Achievements

PHS1 was shown to phosphorylate Thr349 of alpha-tubulin, and the phosphorylated tubulin does not polymerize to microtubule polymer. In plant cells, the phosphatase domain suppresses the kinase domain of PHS1. In response to environmental stress (especially hyperosmotic stress), this suppression is cancelled and the kinase is activated. Liverwort and Chlamydomonas possess PHS1, which is activated by salt and hyperosmotic stresses. In vitro experiments with recombinant proteins show that PHS1 has basal kinase activity, which is directly inactivated by the MPK phosphatase activity within PHS1.

Free Research Field

植物分子細胞生物学