Correction
for
Philipova and Whitaker, J Cell Sci 118 (24) 5767-5776.
First published online April 24, 2006
Journal of Cell Science 119, 1973 (2006)
Published by The Company of Biologists 2006
Author Correction
Philipova, R. and Whitaker, M. (2005). Active ERK1 is dimerized in vivo: bisphosphodimers generate peak kinase activity and monophosphodimers maintain basal ERK1 activity. J. Cell Sci. 118, 5767-5776.
The authors would like to correct an error that occurred when they composed Fig. 2B. The revised figure panel and legend are shown below.
(B) Sea urchin embryos. Active ERK1 was immunoprecipitated during the first mitotic cell cycle at time points that corresponded to maximum (6 min, NEB) and minimum activity (Unfertilized, 30 min) using an anti-dualphosphorylated ERK antibody and detected by western blotting with a second, different anti-dualphosphorylated ERK antibody or with an anti-MEK antibody (NEB sample). Arrows, active ERK1 dimers. Cell extract: whole-cell extracts are rich in ERK1 monomers as a western blot of a 30 minute post-fertilization cell extract detected with anti-ERK antibody demonstrates. It was necessary to load 150 µg total cellular protein in order to obtain a detectable band at 91 kDa for comparison with the anti-dualphosphorylated ERK antibody immunoprecipitate. The positions of molecular mass markers are shown.
