ArticleJournal of molecular evolution1996
Molecular evolution of the metazoan protein kinase C multigene family.
Article in Journal of molecular evolution, 1996. 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, 44 citations in OpenAlex.
- A sponge homolog of BRMS1 reveals ancient origin of metastasis-suppressing functions.BMC biology · 2026Article
- Transfection of Sponge Cells and Intracellular Localization of Cancer-Related MYC, RRAS2, and DRG1 Proteins.Marine drugs · 2023Article
- Structure and function of cancer-related developmentally regulated GTP-binding protein 1 (DRG1) is conserved between sponges and humans.Scientific reports · 2022Article
- Sponges: A Reservoir of Genes Implicated in Human Cancer.Marine drugs · 2018Review
- Regulation of Chlamydomonas flagella and ependymal cell motile cilia by ceramide-mediated translocation of GSK3.Molecular biology of the cell · 2015Article
- Splice variant PRKC-ζ(-PrC) is a novel biomarker of human prostate cancer.British journal of cancer · 2012Article
- Article
- Evolutionary relationships of Metazoa within the eukaryotes based on molecular data from Porifera.Proceedings. Biological sciences · 1999Article
- Evolutionary relationships of the metazoan beta gamma-crystallins, including that from the marine sponge Geodia cydonium.Proceedings. Biological sciences · 1997Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Protein kinases C (PKCs) comprise closely related Ser/Thr kinases, ubiquitously present in animal tissues; they respond to second messengers, e.g., Ca2+ and/or diacylglycerol, to express their activities. Two PKCs have been sequenced from Geodia cydonium, a member of the lowest multicellular animals, the sponges (Porifera). One sponge G. cydonium PKC, GCPKC1, belongs to the "novel" (Ca2+-independent) PKC (nPKC) subfamily while the second one, GCPKC2, has the hallmarks of the "conventional" (Ca2+-dependent) PKC (cPKC) subfamily. The alignment of the Ser/Thr catalytic kinase domains, of the predicted aa sequences for these cDNAs with respective segments from previously reported sequences, revealed highest homology to PKCs from animals but also distant relationships to Ser/Thr kinases from protozoa, plants, and bacteria. However, a comparison of the complete structures of the sponge PKCs, which are-already-identical to those of nPKCs and cPKCs from higher metazoa, with the structures of protozoan, plant, and bacterial Ser/Thr kinases indicates that the metazoan PKCs have to be distinguished from the nonmetazoan enzymes. These data indicate that metazoan PKCs have a universal common ancestor which they share with the nonmetazoan Ser/Thr kinases with respect to the kinase domain, but they differ from them in overall structural composition.
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