Author

S. Katagiri

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Plant Biology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:Arabidopsis· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Organism:E. coli· 1

Frequent Co-Authors

T. Umezawa· 2 shared Y. Kamiyama· 2 shared D. Takezawa· 1 shared F. Minegishi· 1 shared F. Takahashi· 1 shared H. Matsuura· 1 shared H. Takase· 1 shared K. Hirata· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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2 shared papersPlant Biology

T. Umezawa

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Author profile →

3 papers

Recent·Most cited

Hyperosmolarity-induced suppression of group B1 Raf-like protein kinases modulates drought-growth trade-off in Arabidopsis

Y. Kamiyama, S. Katagiri, K. Yamashita, Y. Li, H. Takase, T. Umezawa

The paper identifies Raf13 and IREH1 as growth-promoting kinases suppressed by PP2A under drought stress, modulating the growth-stress trade-off in Arabidopsis.

bioRxiv · Jun 23, 2023 · PreprintPlant Biology

Mechanistic insights into intramembrane proteolysis by E. coli site-2 protease homolog RseP

Y. Imaizumi, K. Takanuki, T. Miyake, M. Takemoto, K. Hirata, M. Hirose, R. Oi, T. Kobayashi, K. Miyoshi, R. Aruga, T. Yokoyama, S. Katagiri, H. Matsuura, K. Iwasaki, T. Kato, , T. Nogi

This study elucidates the mechanism of intramembrane proteolysis by E. coli RseP through crystal structures and mutational analysis, revealing a gating mechanism for substrate entry.

bioRxiv · Jan 31, 2022Biochemistry

SNF1-related protein kinase 2 directly regulate group C Raf-like protein kinases in abscisic acid signaling

Y. Kamiyama, M. Hirotani, S. Ishikawa, F. Minegishi, S. Katagiri, F. Takahashi, M. Nomoto, K. Ishikawa, Y. Kodama, Y. Tada, D. Takezawa, S. C. Peck, K. Shinozaki, T. Umezawa

This study identifies Raf36 as a SnRK2-interacting kinase that negatively regulates ABA responses and is directly phosphorylated by SnRK2s, revealing a new phosphosignaling pathway in ABA signaling.

bioRxiv · Feb 4, 2020 · PreprintPlant Biology