ArticleCell communication and signaling : CCS2018
Systems level expression correlation of Ras GTPase regulators.
Article in Cell communication and signaling : CCS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 9 citations in OpenAlex.
- LINC01996 suppresses non-small cell lung cancer proliferation and metastasis by orchestrating the miR-12115/CNRIP1/Ras signaling axis.Clinical & experimental metastasis · 2026Article
- A RAC-GEF network critical for early intestinal tumourigenesis.Nature communications · 2021Article
- The Regulation of Intestinal Mucosal Barrier by Myosin Light Chain Kinase/Rho Kinases.International journal of molecular sciences · 2020Review
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Authors and funding
8 authors at 5 institutions in 4 countries.
Funding
Abstract
backgroundProteins of the ubiquitously expressed core proteome are quantitatively correlated across multiple eukaryotic species. In addition, it was found that many protein paralogues exhibit expression anticorrelation, suggesting that the total level of protein with a given functionality must be kept constant.
methodsWe performed Spearman's rank correlation analyses of gene expression levels for the RAS GTPase subfamily and their regulatory GEF and GAP proteins across tissues and across individuals for each tissue. A large set of published data for normal tissues from a wide range of species, human cancer tissues and human cell lines was analysed.
resultsWe show that although the multidomain regulatory proteins of Ras GTPases exhibit considerable tissue and individual gene expression variability, their total amounts are balanced in normal tissues. In a given tissue, the sum of activating (GEFs) and deactivating (GAPs) domains of Ras GTPases can vary considerably, but each person has balanced GEF and GAP levels. This balance is impaired in cell lines and in cancer tissues for some individuals.
conclusionsOur results are relevant for critical considerations of knock out experiments, where functionally related homologs may compensate for the down regulation of a protein.
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