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Eukaryotic Cell, June 2008, p. 958-966, Vol. 7, No. 6
1535-9778/08/$08.00+0 doi:10.1128/EC.00442-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Bohye Kim,
Nam-Sihk Lee,
Sudhakar Veeranki, and
Leung Kim*
Department of Biological Sciences, Florida International University, Miami, Florida 33199
Received 5 December 2007/ Accepted 1 April 2008
The novel Dictyostelium phosphatase MPL1 contains six leucine-rich repeats at the amino-terminal end and a phosphatase domain at the carboxyl end. Similarly architectured phosphatases exist among other protozoa, such as Entamoeba histolytica, Leishmania major, and Trypanosoma cruzi. MPL1 was strongly induced after 5 h of development; ablation by homologous recombination led to defective streaming and aggregation during development. In addition, cyclic AMP (cAMP)-pulsed mpl1– cells showed reduced random and directional motility. At the molecular level, mpl1– cells displayed higher prestimulus and persistent poststimulus ERK2 phosphorylation in response to cAMP stimulation. Consistent with their phenotype of persistent ERK2 phosphorylation, mpl1– cells also displayed an aberrant pattern of cAMP production, resembling that of the regA– cells. Reintroduction of a full-length MPL1 into mpl1– cells restored aggregation, ERK2 regulation, random and directional motility, and cAMP production similar to wild-type cells. We propose that MPL1 is a novel phosphatase essential for proper regulation of ERK2 phosphorylation and optimal motility during development.
Published ahead of print on 11 April 2008.
M.R. and B.K. contributed equally to this work.
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