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- Title
Phosphftidic Acid Induces Actin Polymerization by Activating Protein Kinases in Soybean Cells.
- Authors
Lee, Sunlin; Park, Jumok; Lee, Youngsook
- Abstract
Phosphatidic acid (PA) levels rise in response to wounding, stress and elicitors, suggesting that it mediates defense responses in plants. During such responses, actin filaments are altered. Since PA induces actin polymerization in animal ceils we examined its effect on actin structures in suspension-cultured soybean cells. PA caused a three to four (old increase in cells containing filamentous actin. Immunoblotting with anti-actin antibody showed that actin polymerized within 30 min of treatment. The effect of PA on actin polymerization appears to be mediated by prorein kinases because: 1) the effect was suppressed by staurosporin, a general protein kinase inhibitor, and by the protein kinase C-specific inhibitor, calphostin, 2) calyculin A, an inhibitor of protein phosphatasc 1 and 2A, mimicked the effect of PA on act[n polymerization, and 3) PA activated protein kinases in soybean cells. We suggest that a 54 kDa Ca&sup 2+;-dependent protein kinase may transduce the PA signal because EGTA inhibited the 54 kDa kinase and the PA-induced actin polymerization, and similar protein kinases have been reported to co-localize with and regulate actin filaments. Our results support the role of PA as a signal mediator and identify actin as a downstream target of PA.
- Subjects
POLYMERIZATION; CHEMICAL reactions; ACTIN; PROTEIN kinases; PLANTS
- Publication
Molecules & Cells (Springer Nature), 2003, Vol 15, Issue 3, p313
- ISSN
1016-8478
- Publication type
Article
- DOI
10.1016/s1016-8478(23)13743-5