ArticleThe Journal of biological chemistry2009
The protein scaffold NHERF-1 controls the amplitude and duration of localized protein kinase D activity.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
25 citing papers in PubMed, 46 citations in OpenAlex.
- Effect of PRKD3 on cell cycle in gastric cancer progression and downstream regulatory networks.Medical oncology (Northwood, London, England) · 2025Article
- Membrane trafficking in breast cancer progression: protein kinase D comes into play.Frontiers in cell and developmental biology · 2023Review
- Decoding the Cardiac Actions of Protein Kinase D Isoforms.Molecular pharmacology · 2021Review
- Protein kinase D displays intrinsic Tyr autophosphorylation activity: insights into mechanism and regulation.FEBS letters · 2018Article
- Protein kinase D activation induces mitochondrial fragmentation and dysfunction in cardiomyocytes.The Journal of physiology · 2018Article
- Protein kinase D signaling in cancer: A friend or foe?Biochimica et biophysica acta. Reviews on cancer · 2017Review
- Emergency Spatiotemporal Shift: The Response of Protein Kinase D to Stress Signals in the Cardiovascular System.Frontiers in pharmacology · 2017Review
- Phos-tag SDS-PAGE resolves agonist- and isoform-specific activation patterns for PKD2 and PKD3 in cardiomyocytes and cardiac fibroblasts.Journal of molecular and cellular cardiology · 2016Article
- Protein kinase d inhibitors uncouple phosphorylation from activity by promoting agonist-dependent activation loop phosphorylation.Chemistry & biology · 2015Article
- The protein kinase D1 COOH terminus: marker or regulator of enzyme activity?American journal of physiology. Cell physiology · 2014Article
- Imaging kinase activity at protein scaffolds.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Protein kinase C pharmacology: refining the toolbox.The Biochemical journal · 2013Review
- Gβγ-mediated activation of protein kinase D exhibits subunit specificity and requires Gβγ-responsive phospholipase Cβ isoforms.Cell communication and signaling : CCS · 2013Article
- Lysophospholipid receptor activation of RhoA and lipid signaling pathways.Biochimica et biophysica acta · 2013Review
- Shedding light on local kinase activation.BMC biology · 2012Article
- Regulation of protein kinase D1 activity.Molecular pharmacology · 2012Review
- Protein kinase Cα promotes cell migration through a PDZ-dependent interaction with its novel substrate discs large homolog 1 (DLG1).The Journal of biological chemistry · 2011Article
- Emerging roles of protein kinase D1 in cancer.Molecular cancer research : MCR · 2011Review
- Protein kinase D: coupling extracellular stimuli to the regulation of cell physiology.EMBO reports · 2011Review
- Protein kinase D signaling: multiple biological functions in health and disease.Physiology (Bethesda, Md.) · 2011Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Protein kinase D (PKD) transduces an abundance of signals downstream of diacylglycerol production. The mammalian PKD family consists of three isoforms, PKD1, PKD2, and PKD3; of these PKD1 and PKD2 contain PDZ-binding motifs at their carboxyl termini. Here we show that membrane-localized NHERF scaffold proteins provide a nexus for tightly controlled PKD signaling via a PDZ domain interaction. Using a proteomic array containing 96 purified PDZ domains, we have identified the first PDZ domain of NHERF-1 as an interaction partner for the PDZ-binding motifs of both PKD1 and PKD2. A fluorescence resonance energy transfer-based translocation assay reveals a transient association of PKD1 and PKD2 with NHERF-1 in live cells that is triggered by phorbol ester stimulation and, importantly, differs strikingly from the sustained translocation to plasma membrane. Targeting a fluorescence resonance energy transfer-based kinase activity reporter for PKD to NHERF scaffolds reveals a unique signature of PKD activation at the scaffold that is distinct from that of general cytosolic or plasma membrane activity. Specifically, agonist-evoked activation of PKD at the scaffold is rapid and sustained but blunted in magnitude when compared with cytosolic PKD. Thus, live cell imaging of PKD activity demonstrates ultrasensitive control of kinase signaling at the scaffold compared with bulk activity in the cytosol or at the plasma membrane.
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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.