Regulation of wound-responsive calcium-dependent protein kinase from maize (ZmCPK11) by phosphatidic acid.

Abstract:

:In plant cells, phospholipids are not only membrane components but also act as second messengers interacting with various proteins and regulating diverse cellular processes, including stress signal transduction. Here, we report studies on the effects of various phospholipids on the activity and expression of maize wound-responsive calcium-dependent protein kinase (ZmCPK11). Our results revealed that in leaves treated with n-butanol, a potent inhibitor of phosphatidic acid (PA) synthesis catalyzed by phospholipase D, a significant decrease of ZmCPK11 activity was observed, indicating contribution of PA in the kinase activation. Using lipid binding assays, we demonstrate that among various phospholipids only saturated acyl species (16:0 and 18:0) of phosphatidic acid are able to bind to ZmCPK11. Saturated acyl species of PA are also able to stimulate phosphorylation of exogenous substrates by ZmCPK11 and autophosphorylation of the kinase. The level of ZmCPK11 autophosphorylation is correlated with its enzymatic activity. RT-PCR analysis showed that transcript level of ZmCPK11 in maize leaves increased in response to PA treatment. The influence of PA on the activity and transcript level of ZmCPK11 suggests an involvement of this kinase in a PA-mediated wound signal transduction pathway.

journal_name

Acta Biochim Pol

journal_title

Acta biochimica Polonica

authors

Klimecka M,Szczegielniak J,Godecka L,Lewandowska-Gnatowska E,Dobrowolska G,Muszyńska G

subject

Has Abstract

pub_date

2011-01-01 00:00:00

pages

589-95

issue

4

eissn

0001-527X

issn

1734-154X

pii

20110081

journal_volume

58

pub_type

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