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Conserved cross‐interactions in Drosophila and Xenopus between Ras/MAPK signaling and the dual‐specificity phosphatase MKP3
Author(s) -
Gómez Ana Ruiz,
LópezVarea Ana,
Molnar Cristina,
de la CalleMustienes Elisa,
RuizGómez Mar,
GómezSkarmeta José Luis,
de Celis Jose F.
Publication year - 2005
Publication title -
developmental dynamics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.634
H-Index - 141
eISSN - 1097-0177
pISSN - 1058-8388
DOI - 10.1002/dvdy.20227
Subject(s) - biology , xenopus , drosophila (subgenus) , phosphatase , microbiology and biotechnology , dusp6 , dual specificity phosphatase , mapk/erk pathway , protein phosphatase 2 , signal transduction , phosphorylation , genetics , gene
The extracellular signal‐regulated kinase (ERK) is a key transducer of the epidermal growth factor receptor (EGFR) and fibroblast growth factor receptor (FGFR) signaling pathways, and its function is required in multiple processes during animal development. The activity of ERK depends on the phosphorylation state of conserved threonine and tyrosine residues, and this state is regulated by different kinases and phosphatases. A family of phosphatases with specificity toward both threonine and tyrosine residues in ERK (dual‐specificity phosphatases) play a conserved role in its dephosphorylation and consequent inactivation. Here, we characterize the function of the dual‐specificity phosphatase MKP3 in Drosophila EGFR and Xenopus FGFR signaling. The function of MKP3 is required during Drosophila wing vein formation and Xenopus anteroposterior neural patterning. We find that the expression of the MKP3 gene is localized in places of high EGFR and FGFR signaling. Furthermore, this restricted expression depends on ERK function both in Drosophila and Xenopus , suggesting that MKP3 constitutes a conserved negative feedback loop on the activity of the Ras/ERK signaling pathway. Developmental Dynamics 232:695–708, 2005. © 2005 Wiley‐Liss, Inc.