Conserved Domains Subserve Novel Mechanisms and Functions in DKF-1, a Caenorhabditis elegans Protein Kinase D
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TL;DR: C1 domains positively regulated phosphotransferase activity by docking DKF-1 with pools of activating lipid and displayed novel properties indicative of functional malleability (plasticity) by studying Caenorhabditis elegans D kinase family-1.
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About: This article is published in Journal of Biological Chemistry. The article was published on 30 Jun 2006. and is currently open access. The article focuses on the topics: Kinase activity & Mitogen-activated protein kinase kinase.
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Citations
Protein kinase D signaling in cancer: A friend or foe?
TL;DR: This review has provided a comprehensive review of the reported tumor promoting or tumor suppressive functions of PKD in several major cancer types and discussed the discrepancies that have been raised on PKD as a major regulator of malignant transformation.
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Protein kinase D1 autophosphorylation via distinct mechanisms at Ser744/Ser748 and Ser916.
TL;DR: This study exposes a novel role for Ser916 and/or Ser748 autophosphorylation to terminate the cellular PKD1 signaling response and implicates PKD 1-Ser744 phosphorylation in the phorbol 12-myristate 13-acetate-dependent mechanism that increasesPKD1 activity toward physiologically relevant substrates.
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Properties, regulation, and in vivo functions of a novel protein kinase D: Caenorhabditis elegans DKF-2 links diacylglycerol second messenger to the regulation of stress responses and life span.
TL;DR: The results suggest a mechanism for increased longevity and show that a PKD links DAG signals to regulation of stress responses and life span.
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A protein kinase C/protein kinase D pathway protects LNCaP prostate cancer cells from phorbol ester-induced apoptosis by promoting ERK1/2 and NF-κB activities
TL;DR: The data indicate that PKD1 is activated and downregulated by PMA through a PKC-dependent ubiquitin-proteasome degradation pathway, and the activation of PKD 1 or PKD2 counteracts PMA-induced apoptosis by promoting downstream ERK1/2 and NF-κB activities in LNCaP prostate cancer cells.
Neuronal and Intestinal Protein Kinase D Isoforms Mediate Na+ (Salt Taste)–Induced Learning
TL;DR: It is shown that pathways containing EGL-8–TPA-1–DKF-2 enable learning and behavioral plasticity by receiving, transmitting, and cooperatively integrating environmental signals targeted to both neurons and intestine.
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References
The Protein Kinase Complement of the Human Genome
TL;DR: The protein kinase complement of the human genome is catalogued using public and proprietary genomic, complementary DNA, and expressed sequence tag sequences to provide a starting point for comprehensive analysis of protein phosphorylation in normal and disease states and a detailed view of the current state of human genome analysis through a focus on one large gene family.
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Protein kinase C and lipid signaling for sustained cellular responses.
TL;DR: It is now becoming evident that stimulation of a cell surface receptor initiates a degradation cascade of various membrane lipid constituents that has potentials to induce, intensify, and prolong the activation of protein kinase C that is needed for sustained cellular responses.
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PDK1, the master regulator of AGC kinase signal transduction.
TL;DR: Recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (PDK1), which phosphorylates and activates the AGC kinase members regulated by PI 3-kinase, are reviewed.
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Signal-dependent membrane targeting by pleckstrin homology (PH) domains
TL;DR: The possibility that membrane targeting by PH domains with low affinity for phosphoinositides could be driven by alteration of their oligomeric state and thus the avidity of their membrane binding is discussed.
Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
TL;DR: Two amino acids in the PLC-delta 1 PH domain that contact Ins(1,4,5)P3 have counterparts in the Bruton's tyrosine kinase (Btk) PH domain, suggesting a mechanism for loss of function in Btk mutants.
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