ArticleCellular signalling2015
The Dictyostelium MAPK ERK1 is phosphorylated in a secondary response to early developmental signaling.
Article in Cellular signalling, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 20 citations in OpenAlex.
- Related Dictyostelium G protein subunits Gα1 and Gα2 have different roles in chemotaxis and transcription factor regulation.BMC molecular and cell biology · 2025Article
- Two endogenousProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Regulatory differences between atypical and typical MAP kinases in Dictyostelium discoideum.Cellular signalling · 2025Article
- Atypical MAP kinases - new insights and directions from amoeba.Journal of cell science · 2023Review
- An integrated, cross-regulation pathway model involving activating/adaptive and feed-forward/feed-back loops for directed oscillatory cAMP signal-relay/response during the development ofFrontiers in cell and developmental biology · 2023Article
- An atypical MAPK regulates translocation of a GATA transcription factor in response to chemoattractant stimulation.Journal of cell science · 2022Article
- MAPK docking motif in the Dictyostelium Gα2 subunit is required for aggregation and transcription factor translocation.Cellular signalling · 2021Article
- Article
- Article
- Mitogen-activated protein kinase regulation of the phosphodiesterase RegA in earlyMicrobiology (Reading, England) · 2020Article
- Caffeine inhibits PI3K and mTORC2 in Dictyostelium and differentially affects multiple other cAMP chemoattractant signaling effectors.Molecular and cellular biochemistry · 2019Article
- Early Evolution of the Mitogen-Activated Protein Kinase Family in the Plant Kingdom.Scientific reports · 2019Article
- An endogenous chemorepellent directs cell movement by inhibiting pseudopods at one side of cells.Molecular biology of the cell · 2019Article
- Dictyostelium Erk2 is an atypical MAPK required for chemotaxis.Cellular signalling · 2018Article
- Extracellular polyphosphate signals through Ras and Akt to primeJournal of cell science · 2017Article
- Phylogenetic evidence for the modular evolution of metazoan signalling pathways.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Previous reports have suggested that the two mitogen-activated protein kinases (MAPKs) in Dictyostelium discoideum, ERK1 and ERK2, can be directly activated in response to external cAMP even though these MAPKs play different roles in the developmental life cycle. To better characterize MAPK regulation, the levels of phosphorylated MAPKs were analyzed in response to external signals. Only ERK2 was rapidly phosphorylated in response to the chemoattractants, cAMP and folate. In contrast, the phosphorylation of ERK1 occurred as a secondary or indirect response to these stimuli and this phosphorylation was enhanced by cell-cell interactions, suggesting that other external signals can activate ERK1. The phosphorylation of ERK1 or ERK2 did not require the function of the other MAPK in these responses. Folate stimulation of a chimeric population of erk1- and gα4- cells revealed that the phosphorylation of ERK1 could be mediated through an intercellular signal other than folate. Loss of ERK1 function suppressed the developmental delay and the deficiency in anterior cell localization associated with gα5- mutants suggesting that ERK1 function can be down regulated through Gα5 subunit-mediated signaling. However, no major changes in the phosphorylation of ERK1 were observed in gα5- cells suggesting that the Gα5 subunit signaling pathway does not regulate the phosphorylation of ERK1. These findings suggest that the activation of ERK1 occurs as a secondary response to chemoattractants and that other cell-cell signaling mechanisms contribute to this activation. Gα5 subunit signaling can down regulate ERK1 function to promote prestalk cell development but not through major changes to the level of phosphorylated ERK1.
Indexed as
Identifiers
What OpenQuestion holds
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.