Tyrosine phosphorylation as a signaling component for plant improvement

• 발행기관: (사)한국식물생명공학회
• 저자명: Youn-Il Park Hyo-Sik Yang Man-Ho Oh
• 간행물 정보: 『Journal of Plant Biotechnology』42권 4호, 277~283쪽, 전체 7쪽
• 주제분류: 농수해양 > 기타농수해양
• 파일형태: PDF
• 발행일자: 2015.12.31

영문 초록

Plant genome analyses, including Arabidopsis thaliana showed a large gene family of plant receptor kinases with various extracellular ligand-binding domain. Now intensively studies to understand physiological and cellular functions for higher plant receptor kinases in diverse and complex biological processes including plant growth, development, ligands perception including steroid hormone and plant-microbe interactions. Brassinosteroids (BRs) as a one of well know steroid hormone are plant growth hormones that control biomass accumulation and also tolerance to many biotic and abiotic stress conditions and hence are of relevance to agriculture. BRI1 receptor kinase, which is localized in plasma membrane in the cell sense BRs and it bind to a receptor protein known as BRASSINOSTEROID INSENSITIVE 1 (BRI1). Recently, we reported that BRI1 and its co-receptor, BRI1-ASSOCIATED KINASE (BAK1) autophosphorylated on tyrosine residue (s) in vitro and in vivo and thus are dual-specificity kinases. Other plant receptor kinases are also phosphorylated on tyrosine residue (s). Post-translational modifications (PTMs) can be studied by altering the residue modified by directed mutagenesis to mimic the modified state or to prevent the modification. These approaches are useful to not only characterize the regulatory role of a given modification, but may also provide opportunities for plant improvement.

목차

Introduction

Tyrosine phosphorylation of plant proteins including

receptor kinases

Dual-specificity of receptor kinases

Possible role of tyrosine phosphorylation in

Arabidopsis thaliana

Conclusions

Acknowledgements

References

키워드

Post-translational modification Brassinosteroids BRASSINOSTEROID INSENSITIVE 1 Plant Receptor Kinases BRI1-ASSOCIATED KINASE1 Tyrosine phosphorylation