ArticleStructure (London, England : 1993)2008
Structure of the human protein kinase MPSK1 reveals an atypical activation loop architecture.
Article in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 37 citations in OpenAlex.
- AAK1-mediated phosphorylation of PDLIM5 and Talin1 promotes focal adhesion disassembly to accelerate cell migration.Nature communications · 2026Article
- Current thoughts on cellular functions of numb-associated kinases.Molecular biology reports · 2023Review
- Article
- Kinases on Double Duty: A Review of UniProtKB Annotated Bifunctionality within the Kinome.Biomolecules · 2022Review
- Conservation of the unusual dimeric JmjC fold of JMJD7 from Drosophila melanogaster to humans.Scientific reports · 2022Article
- Developmentally regulated GTPases: structure, function and roles in disease.Cellular and molecular life sciences : CMLS · 2021Review
- A kinase cascade on the yeast lysosomal vacuole regulates its membrane dynamics: conserved kinase Env7 is phosphorylated by casein kinase Yck3.The Journal of biological chemistry · 2020Article
- The STK16 inhibitor STK16-IN-1 inhibits non-adrenergic and non-neurogenic smooth muscle contractions in the human prostate and the human male detrusor.Naunyn-Schmiedeberg's archives of pharmacology · 2020Article
- SGC-AAK1-1: A Chemical Probe Targeting AAK1 and BMP2K.ACS medicinal chemistry letters · 2020Article
- Tyr198 is the Essential Autophosphorylation Site for STK16 Localization and Kinase Activity.International journal of molecular sciences · 2019Article
- Serine/Threonine Protein Kinase STK16.International journal of molecular sciences · 2019Review
- Structural Basis for the Inhibition of Cyclin G-Associated Kinase by Gefitinib.ChemistryOpen · 2018Article
- A Serine/Threonine Kinase 16-Based Phospho-Proteomics Screen Identifies WD Repeat Protein-1 As A Regulator Of Constitutive Secretion.Scientific reports · 2018Article
- STK16 regulates actin dynamics to control Golgi organization and cell cycle.Scientific reports · 2017Article
- Family-wide Structural Analysis of Human Numb-Associated Protein Kinases.Structure (London, England : 1993) · 2016Article
- Serine/threonine kinase 16 and MAL2 regulate constitutive secretion of soluble cargo in hepatic cells.The Biochemical journal · 2014Article
- Distinct palmitoylation events at the amino-terminal conserved cysteines of Env7 direct its stability, localization, and vacuolar fusion regulation in S. cerevisiae.The Journal of biological chemistry · 2014Article
- Structure of cyclin G-associated kinase (GAK) trapped in different conformations using nanobodies.The Biochemical journal · 2014Article
- Saccharomyces cerevisiae Env7 is a novel serine/threonine kinase 16-related protein kinase and negatively regulates organelle fusion at the lysosomal vacuole.Molecular and cellular biology · 2013Article
- Rbg1-Tma46 dimer structure reveals new functional domains and their role in polysome recruitment.Nucleic acids research · 2012Article
Corrections and comments
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Authors and funding
10 authors at 6 institutions in 3 countries.
Funding
Abstract
The activation segment of protein kinases is structurally highly conserved and central to regulation of kinase activation. Here we report an atypical activation segment architecture in human MPSK1 comprising a beta sheet and a large alpha-helical insertion. Sequence comparisons suggested that similar activation segments exist in all members of the MPSK1 family and in MAST kinases. The consequence of this nonclassical activation segment on substrate recognition was studied using peptide library screens that revealed a preferred substrate sequence of X-X-P/V/I-phi-H/Y-T*-N/G-X-X-X (phi is an aliphatic residue). In addition, we identified the GTPase DRG1 as an MPSK1 interaction partner and specific substrate. The interaction domain in DRG1 was mapped to the N terminus, leading to recruitment and phosphorylation at Thr100 within the GTPase domain. The presented data reveal an atypical kinase structural motif and suggest a role of MPSK1 regulating DRG1, a GTPase involved in regulation of cellular growth.
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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.