Location of Repository

MPL1, a Novel Phosphatase with Leucine-Rich Repeats, Is Essential for Proper ERK2 Phosphorylation and Cell Motility▿

By Marbelys Rodriguez, Bohye Kim, Nam-Sihk Lee, Sudhakar Veeranki and Leung Kim

Abstract

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

Topics: Articles
Publisher: American Society for Microbiology (ASM)
OAI identifier: oai:pubmedcentral.nih.gov:2446661
Provided by: PubMed Central
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • http://www.pubmedcentral.nih.g... (external link)
  • Suggested articles


    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.