ArticleJournal of cancer biology & research2014
Cross-Phosphorylation and Interaction between Src/FAK and MAPKAP5/PRAK in Early Focal Adhesions Controls Cell Motility.
Article in Journal of cancer biology & research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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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.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
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- β-elemene inhibits non-small cell lung cancer cell migration and invasion by inactivating the FAK-Src pathway.Experimental and therapeutic medicine · 2021Article
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- Does the prenatal bisphenol A exposure alter DNA methylation levels in the mouse hippocampus?: An analysis using a high-sensitivity methylome technique.Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2018Article
- L290P/V mutations increase ERK3's cytoplasmic localization and migration/invasion-promoting capability in cancer cells.Scientific reports · 2017Article
- Decreased TRPM7 inhibits activities and induces apoptosis of bladder cancer cells via ERK1/2 pathway.Oncotarget · 2016Article
- A novel role for atypical MAPK kinase ERK3 in regulating breast cancer cell morphology and migration.Cell adhesion & migration · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
P38-regulated and activated kinase (PRAK/MAPKAPK5) is a serine/threonine kinase which lies downstream of the p38 and ERK3/4 MAP kinase pathways. PRAK plays diverse roles in the processes of cell growth, nutrient starvation response, programmed cell death, senescence and motility. PRAK has been shown to both promote and inhibit cell motility in different contexts. The pro-motility functions of PRAK are attributed mainly to cytoskeletal rearrangement occurring downstream of its phosphorylated substrate HSP27; however, it was recently shown that PRAK is required for motility in endothelial cells upstream of Focal adhesion kinase (FAK). Along with Src, FAK functions as a mediator of motility signaling through the phosphorylation of substrates in focal adhesions. Here, we show that PRAK, initially identified as a FAK substrate in an
Indexed as
Identifiers
26042227PMC4450445W2405076250What 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.