Modulation of plant growth in vivo and identification of kinase substrates using an analog-sensitive variant of CYCLIN-DEPENDENT KINASE A;1.

Date publication

septembre 2016

Journal

BMC plant biology

Auteurs

Membres identifiés du Cancéropôle Est :
Mr HAMMANN Philippe

Tous les auteurs :
Harashima H, Dissmeyer N, Hammann P, Nomura Y, Kramer K, Nakagami H, Schnittger A

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/27669979

Résumé

Modulation of protein activity by phosphorylation through kinases and subsequent de-phosphorylation by phosphatases is one of the most prominent cellular control mechanisms. Thus, identification of kinase substrates is pivotal for the understanding of many - if not all - molecular biological processes. Equally, the possibility to deliberately tune kinase activity is of great value to analyze the biological process controlled by a particular kinase.

Référence

BMC Plant Biol.. 2016 Sep 26;16(1):209