Chapter title |
CDPK Activation in PRR Signaling
|
---|---|
Chapter number | 14 |
Book title |
Plant Pattern Recognition Receptors
|
Published in |
Methods in molecular biology, February 2017
|
DOI | 10.1007/978-1-4939-6859-6_14 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6858-9, 978-1-4939-6859-6
|
Authors |
Heike Seybold, Marie Boudsocq, Tina Romeis |
Editors |
Libo Shan, Ping He |
Abstract |
Calcium-dependent protein kinases undergo a rapid biochemical activation in response to an intracellular Ca increase induced by the PRR-dependent perception of a pathogen-related stimulus. Based on SDS gel resolution, the in-gel kinase assay allows the analysis of multiple in vivo protein samples in parallel, combining the advantage of protein separation according to molecular mass with the activity read-out of a protein kinase assay. It thus enables to follow the transient CDPK activation and inactivation in response to in vivo elicitation with a time-wise resolution. In addition, changes of CDPK phosphorylation activity often correlate with slight shifts in the enzyme's apparent molecular mass, indicating posttranslational modifications and a conformational change of the active enzyme compared to its inactive resting form. These band shifts can be detected by a simple immunoblotting to monitor CDPK activation. |
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