ArticleWorld journal of biological chemistry2012
Septin 8 is an interaction partner and in vitro substrate of MK5.
Article in World journal of biological chemistry, 2012. 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, 25 citations in OpenAlex.
- Proteomic landscape profiling of primary prostate cancer reveals a 16-protein panel for prognosis prediction.Cell reports. Medicine · 2024Article
- TLK1-mediated MK5-S354 phosphorylation drives prostate cancer cell motility and may signify distinct pathologies.Molecular oncology · 2022Article
- Sept8/SEPTIN8 involvement in cellular structure and kidney damage is identified by genetic mapping and a novel human tubule hypoxic model.Scientific reports · 2021Article
- Septin-2 is overexpressed in epithelial ovarian cancer and mediates proliferation via regulation of cellular metabolic proteins.Oncotarget · 2019Article
- Phosphorylation of Pnut in the Early Stages ofG3 (Bethesda, Md.) · 2018Article
- The novel RAGE interactor PRAK is associated with autophagy signaling in Alzheimer's disease pathogenesis.Molecular neurodegeneration · 2016Article
- Septin functions in organ system physiology and pathology.Biological chemistry · 2014Review
- The Role of Mitogen-Activated Protein Kinase-Activated Protein Kinases (MAPKAPKs) in Inflammation.Genes · 2013Article
- Phosphoregulation of the septin cytoskeleton in neuronal development and disease.Cytoskeleton (Hoboken, N.J.)Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
aimTo identify novel substrates for the mitogen-activated protein kinase-activated protein kinase 5 (MK5).
methodsYeast two-hybrid screening with MK5 as bait was used to identify novel possible interaction partners. The binding of putative partner was further examined by glutathione S-transferase (GST) pull-down, co-immunoprecipitation and fluorescence resonance energy transfer (FRET) analysis. In vitro kinase and peptide array assays were used to map MK5 phosphoacceptor sites on the new partner. Confocal microscopy was performed to study the subcellular localization of MK5 and its partners.
resultsSeptin 8 was identified as a novel interaction partner for MK5 by yeast two-hybrid screening. This interaction was confirmed by GST pull-down, co-immunoprecipitation and FRET analysis. Septin 5, which can form a complex with septin 8, did not interact with MK5. Serine residues 242 and 271 on septin 8 were identified as in vitro MK5 phosphorylation sites. MK5 and septin 8 co-localized in the perinuclear area and in cell protrusions. Moreover, both proteins co-localized with vesicle marker synaptophysin.
conclusionSeptin 8 is a bona fide interaction partner and in vitro substrate for MK5. This interaction may be implicated in vesicle trafficking.
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