ArticleEukaryotic cell2006
EppA, a putative substrate of DdERK2, regulates cyclic AMP relay and chemotaxis in Dictyostelium discoideum.
Article in Eukaryotic cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Atypical MAP kinases - new insights and directions from amoeba.Journal of cell science · 2023Review
- An atypical MAPK regulates translocation of a GATA transcription factor in response to chemoattractant stimulation.Journal of cell science · 2022Article
- Mitogen-activated protein kinase regulation of the phosphodiesterase RegA in earlyMicrobiology (Reading, England) · 2020Article
- The Atypical MAP Kinase ErkB Transmits Distinct Chemotactic Signals through a Core Signaling Module.Developmental cell · 2019Article
- Dictyostelium Erk2 is an atypical MAPK required for chemotaxis.Cellular signalling · 2018Article
- Absence of catalytic domain in a putative protein kinase C (PkcA) suppresses tip dominance in Dictyostelium discoideum.Developmental biology · 2015Article
- The Dictyostelium prestalk inducer differentiation-inducing factor-1 (DIF-1) triggers unexpectedly complex global phosphorylation changes.Molecular biology of the cell · 2015Article
- Paxillin and phospholipase D interact to regulate actin-based processes in Dictyostelium discoideum.Eukaryotic cell · 2011Article
- MAPKs in development: insights from Dictyostelium signaling pathways.Biomolecular concepts · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
The mitogen-activated protein kinase DdERK2 is critical for cyclic AMP (cAMP) relay and chemotaxis to cAMP and folate, but the details downstream of DdERK2 are unclear. To search for targets of DdERK2 in Dictyostelium discoideum, 32PO4(3-)-labeled protein samples from wild-type and Dderk2- cells were resolved by 2-dimensional electrophoresis. Mass spectrometry was used to identify a novel 45-kDa protein, named EppA (ERK2-dependent phosphoprotein A), as a substrate of DdERK2 in Dictyostelium. Mutation of potential DdERK2 phosphorylation sites demonstrated that phosphorylation on serine 250 of EppA is DdERK2 dependent. Changing serine 250 to alanine delayed development of Dictyostelium and reduced Dictyostelium chemotaxis to cAMP. Although overexpression of EppA had no significant effect on the development or chemotaxis of Dictyostelium, disruption of the eppA gene led to delayed development and reduced chemotactic responses to both cAMP and folate. Both eppA gene disruption and overexpression of EppA carrying the serine 250-to-alanine mutation led to inhibition of intracellular cAMP accumulation in response to chemoattractant cAMP, a pivotal process in Dictyostelium chemotaxis and development. Our studies indicate that EppA regulates extracellular cAMP-induced signal relay and chemotaxis of Dictyostelium.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.