ArticleThe Journal of cell biology1999
Novel protein kinases Ark1p and Prk1p associate with and regulate the cortical actin cytoskeleton in budding yeast.
Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed.
- Cross-regulations of two connected domains form a mechanical circuit for steady force transmission during clathrin-mediated endocytosis.Cell reports · 2024Article
- Recent progress in discovery of novel AAK1 inhibitors: from pain therapy to potential anti-viral agents.Journal of enzyme inhibition and medicinal chemistry · 2023Review
- Current thoughts on cellular functions of numb-associated kinases.Molecular biology reports · 2023Review
- Spatio-temporal regulation of endocytic protein assembly by SH3 domains in yeast.Molecular biology of the cell · 2023Article
- Eps15/Pan1p is a master regulator of the late stages of the endocytic pathway.The Journal of cell biology · 2022Article
- Phosphorylation of the WH2 domain in yeast Las17/WASP regulates G-actin binding and protein function during endocytosis.Scientific reports · 2021Article
- Spatial regulation of clathrin-mediated endocytosis through position-dependent site maturation.The Journal of cell biology · 2020Article
- Conserved Ark1-related kinases function in a TORC2 signaling network.Molecular biology of the cell · 2020Article
- Quantitative Proteomic Profiling of Marine DiatomFrontiers in microbiology · 2020Article
- The ability of transcription factors to differentially regulate gene expression is a crucial component of the mechanism underlying inversion, a frequently observed genetic interaction pattern.PLoS computational biology · 2019Article
- Target of rapamycin complex 2-dependent phosphorylation of the coat protein Pan1 by Akl1 controls endocytosis dynamics inThe Journal of biological chemistry · 2018Article
- Yeast Aim21/Tda2 both regulates free actin by reducing barbed end assembly and forms a complex with Cap1/Cap2 to balance actin assembly between patches and cables.Molecular biology of the cell · 2018Article
- The fungal myosin I is essential for Fusarium toxisome formation.PLoS pathogens · 2018Article
- The TORC2-Dependent Signaling Network in the Yeast Saccharomyces cerevisiae.Biomolecules · 2017Review
- MoEnd3 regulates appressorium formation and virulence through mediating endocytosis in rice blast fungus Magnaporthe oryzae.PLoS pathogens · 2017Article
- MoCAP proteins regulated by MoArk1-mediated phosphorylation coordinate endocytosis and actin dynamics to govern development and virulence of Magnaporthe oryzae.PLoS genetics · 2017Article
- TOR Complex 2-Regulated Protein Kinase Fpk1 Stimulates Endocytosis via Inhibition of Ark1/Prk1-Related Protein Kinase Akl1 in Saccharomyces cerevisiae.Molecular and cellular biology · 2017Article
- Identifying protein kinase-specific effectors of the osmostress response in yeast.Science signaling · 2017Article
- Growth condition dependency is the major cause of non-responsiveness upon genetic perturbation.PloS one · 2017Article
- Clathrin-mediated endocytosis in budding yeast at a glance.Journal of cell science · 2016Review
18 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
Funding
Abstract
Ark1p (actin regulating kinase 1) was identified as a yeast protein that binds to Sla2p, an evolutionarily conserved cortical actin cytoskeleton protein. Ark1p and a second yeast protein, Prk1p, contain NH2-terminal kinase domains that are 70% identical. Together with six other putative kinases from a number of organisms, these proteins define a new protein kinase family that we have named the Ark family. Lack of both Ark1p and Prk1p resulted in the formation of large cytoplasmic actin clumps and severe defects in cell growth. These defects were rescued by wild-type, but not by kinase-dead versions of the proteins. Elevated levels of either Ark1p or Prk1p caused a number of actin and cell morphological defects that were not observed when the kinase-dead versions were overexpressed instead. Ark1p and Prk1p were shown to localize to actin cortical patches, making these two kinases the first signaling proteins demonstrated to be patch components. These results suggest that Ark1p and Prk1p may be downstream effectors of signaling pathways that control actin patch organization and function. Furthermore, results of double-mutant analyses suggest that Ark1p and Prk1p function in overlapping but distinct pathways that regulate the cortical actin cytoskeleton.
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