ArticleInternational journal of molecular sciences2018
STE20/PAKA Protein Kinase Gene Releases an Autoinhibitory Domain through Pre-mRNA Alternative Splicing in the Dermatophyte
Article in International journal of molecular sciences, 2018. 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, 17 citations in OpenAlex.
- Deciphering the genomic landscape ofMicrobial genomics · 2026Article
- Omics-based dissection of alternative splicing and the regulatory architecture in fungal genomes.Current research in microbial sciences · 2026Review
- The Antidepressant Sertraline Modulates Gene Expression and Alternative Splicing Events in the DermatophyteGenes · 2025Article
- Alternative Splicing inJournal of fungi (Basel, Switzerland) · 2022Article
- Genome-wide identification and functional analysis of circRNAs in Trichophyton rubrum conidial and mycelial stages.BMC genomics · 2022Article
- Peptidase Regulation inFrontiers in microbiology · 2022Article
- State-of-the-Art Dermatophyte Infections: Epidemiology Aspects, Pathophysiology, and Resistance Mechanisms.Journal of fungi (Basel, Switzerland) · 2021Review
- Reassessing the Use of Undecanoic Acid as a Therapeutic Strategy for Treating Fungal Infections.Mycopathologia · 2021Review
- Alternative Splicing in Heat Shock Protein Transcripts as a Mechanism of Cell Adaptation inCells · 2019Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Signaling pathways are highly diverse in filamentous fungi, allowing the cells to receive and process ambient information. Interaction of components from different pathways results in signaling networks. The mitogen-activated protein kinase (MAPK) pathway is dependent on phosphorylation that is accomplished by kinase proteins. Thus, the STE/PAK protein kinase family plays essential roles in MAPK signal transduction, regulating several cellular functions. The STE/PAK protein displays an autoinhibitory (Cdc42/Rac interactive binding-CRIB) domain on its N-terminal portion, which interacts with the C-terminal catalytic kinase domain. Based on current knowledge, for the STE/PAK kinase to be activated, molecular signals (e.g., interaction with the activated form of Rac1 and Cdc42 proteins) or proteolytic cleavage by caspase 3 is necessary. Both mechanisms release the kinase domain from the CRIB interaction. Here, we hypothesize a novel molecular mechanism for the activation of STE20/PAKA kinase in
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