Identification of a putative target for Rho as the serine-threonine kinase protein kinase N
M Amano, H Mukai, Y Ono, K Chihara, T Matsui… - Science, 1996 - science.org
M Amano, H Mukai, Y Ono, K Chihara, T Matsui, Y Hamajima, K Okawa, A Iwamatsu…
Science, 1996•science.orgRho, a Ras-like small guanosine triphosphatase, has been implicated in cytoskeletal
responses to extracellular signals such as lysophosphatidic acid (LPA) to form stress fibers
and focal contacts. The form of RhoA bound to guanosine triphosphate directly bound to and
activated a serine-threonine kinase, protein kinase N (PKN). Activated RhoA formed a
complex with PKN and activated it in COS-7 cells. PKN was phosphorylated in Swiss 3T3
cells stimulated with LPA, and this phosphorylation was blocked by treatment of cells with …
responses to extracellular signals such as lysophosphatidic acid (LPA) to form stress fibers
and focal contacts. The form of RhoA bound to guanosine triphosphate directly bound to and
activated a serine-threonine kinase, protein kinase N (PKN). Activated RhoA formed a
complex with PKN and activated it in COS-7 cells. PKN was phosphorylated in Swiss 3T3
cells stimulated with LPA, and this phosphorylation was blocked by treatment of cells with …
Rho, a Ras-like small guanosine triphosphatase, has been implicated in cytoskeletal responses to extracellular signals such as lysophosphatidic acid (LPA) to form stress fibers and focal contacts. The form of RhoA bound to guanosine triphosphate directly bound to and activated a serine-threonine kinase, protein kinase N (PKN). Activated RhoA formed a complex with PKN and activated it in COS-7 cells. PKN was phosphorylated in Swiss 3T3 cells stimulated with LPA, and this phosphorylation was blocked by treatment of cells with botulinum C3 exoenzyme. Activation of Rho may be linked directly to a serine-threonine kinase pathway.
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