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The NPK1 mitogen-activated protein kinase kinase kinase is a regulator of cell-plate formation in plant cytokinesis

Article Abstract:

Results demonstrate that the tobacco mitogen-activated protein kinase kinase kinase NPK1 is involved in the cytokinesis and its activity follows cell cycle events. Data show that NPK1 is required for the cell plate formation as evidenced by kinase-negative NPK1 mutants' inability to form complete cell plates.

Author: Nishihama, Ryuichi, Ishikawa, Masaki, Araki, Satoshi, Soyano, Takashi, Asada, Tetsuhiro, Machida, Yasunori
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2001
Enzymes, Cell division, Enzyme regulation

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NQK1/NtMEK1 is a MAPKK that acts in the NPK1 MAPKKK-mediated MAPK cascade and is required for plant cytokinesis

Article Abstract:

Research has been conducted on tobacco protein kinase NPK1 which is mitogen-activated protein kinase kinase kinase (MAPKKK) regulating cell plate formation during cytokinesis. The authors report the identification of tobacco NQK1/NtMEK1 and NPK1 as mitogen-activated protein kinase kinase (MAPKK) and mitogen-activated protein kinase (MAPK) doenstream of NPK1.

Author: Nishihama, Ryuichi, Ishikawa, Masaki, Soyano, Takashi, Machida, Yasunori, Morikiyo, Kayoko
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2003
Cells (Biology), Genetic regulation, Cells, Mitosis, Genetic research

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Phosphorylation of NtMAP65-1 by a MAP kinase down-regulates its activity of microtubule bundling and stimulates progression of cytokinesis of tobacco cells

Article Abstract:

The tobacco mitogen-activated protein kinase (MAPK) cascade, which includes MAPK NRK1/NTF6, positively regulates expansion of the cytokinetic machinery known as the phragmoplast, which is followed by the synthesis of cell plates for completion of cell division. The results suggest that phosphorylation of NtMAP65-1 by NRK1/NTF6 also reduces its MT-bundling activity in vivo, which enhances destabilization and turnover of MTs at the phragmoplast equator, perhaps facilitating phragmoplast expansion.

Author: Soyano, Takashi, Machida, Yasunori, Sasabe, Michiko, Itoh, Tomohiko J., Hidaka, Mikiko, Takahashi, Yuji, Sonobe, Seiji, Igarashi, Hisako
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2006
Phosphorylation, Mitogens, Tobacco (Plant)

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Subjects list: Japan, Physiological aspects, Protein kinases, Cytokinesis, Research, Analysis, Genetic aspects
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