scholarly journals Protein kinase D: coupling extracellular stimuli to the regulation of cell physiology

EMBO Reports ◽  
2011 ◽  
Vol 12 (8) ◽  
pp. 785-796 ◽  
Author(s):  
Ya Fu ◽  
Charles S Rubin
Keyword(s):  
Protein Kinase ◽  
Protein Kinase D ◽  
Cell Physiology ◽  
Extracellular Stimuli

scholarly journals Angiotensin II-Mediated Protein Kinase D Activation Stimulates Aldosterone and Cortisol Secretion in H295R Human Adrenocortical Cells

Endocrinology ◽  
2006 ◽  
Vol 147 (12) ◽  
pp. 6046-6055 ◽  
Author(s):  
Damian G. Romero ◽  
Bronwyn L. Welsh ◽  
Elise P. Gomez-Sanchez ◽  
Licy L. Yanes ◽  
Silvia Rilli ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Protein Kinase ◽  
Protein Kinases ◽  
Intracellular Signaling ◽  
Molecular Mechanisms ◽  
Protein Kinase D ◽  
Cell Physiology ◽  
Cortisol Secretion ◽  
Adrenal Cells ◽  
Constitutively Active

Protein kinases are important mediators in intracellular signaling. Angiotensin II is the most important modulator of adrenal zona glomerulosa cell physiology. Angiotensin II regulates steroidogenesis and proliferation among many other metabolic processes. H295R human adrenal cells are a widely used experimental model to study adrenal cell physiology and metabolism. We screened for protein kinase expression levels using the Kinetwork system in H295R cells after 3 h angiotensin II treatment. Protein kinase D (PKD) was the protein kinase that suffers the most dramatic changes. PKD is a member of a new class of serine/threonine protein kinases that is activated by phosphorylation. Our studies indicated that angiotensin II time- and dose-dependently increased PKD phosphorylation, which occurred within 2 min of angiotensin II treatment and at concentrations as low as 1 nm. PKD phosphorylation was also dose-dependently increased by the PKC activator phorbol 12-myristate 13-acetate. Angiotensin II-mediated PKD phosphorylation was blocked by several PKC inhibitors. Furthermore, PKCε translocation inhibitor peptide decreased angiotensin II-mediated PKD phosphorylation, and PKCε down-regulation by RNA interference also decreased PKD phosphorylation mediated by angiotensin II. Cotransfection of constitutively active PKD mutant constructs up-regulated aldosterone synthase and 11β-hydroxylase expression in reporter assays. Constitutively active PKD mutants increased aldosterone and cortisol secretion under angiotensin II stimulatory conditions. This study reveals that PKD is an intracellular signaling mediator of angiotensin II regulation of steroidogenesis in human adrenal cells. These data provide new insights into the molecular mechanisms involved in angiotensin II-induced physiological and pathophysiological events in adrenal cells.

scholarly journals Angiotensin II-activated protein kinase D mediates acute aldosterone secretion

2010 ◽  
Vol 317 (1-2) ◽  
pp. 99-105 ◽  
Author(s):  
Brian A. Shapiro ◽  
Lawrence Olala ◽  
Senthil Nathan Arun ◽  
Peter M. Parker ◽  
Mariya V. George ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Protein Kinase ◽  
Protein Kinase D ◽  
Aldosterone Secretion

scholarly journals Protein kinase D promotes plasticity-induced F-actin stabilization in dendritic spines and regulates memory formation

2015 ◽  
Vol 210 (5) ◽  
pp. 771-783 ◽  
Author(s):  
Norbert Bencsik ◽  
Zsófia Szíber ◽  
Hanna Liliom ◽  
Krisztián Tárnok ◽  
Sándor Borbély ◽  
...  
Keyword(s):  
Synaptic Plasticity ◽  
Protein Kinase ◽  
Dendritic Spines ◽  
Morphological Changes ◽  
Long Term Potentiation ◽  
Memory Formation ◽  
Protein Kinase D

Actin turnover in dendritic spines influences spine development, morphology, and plasticity, with functional consequences on learning and memory formation. In nonneuronal cells, protein kinase D (PKD) has an important role in stabilizing F-actin via multiple molecular pathways. Using in vitro models of neuronal plasticity, such as glycine-induced chemical long-term potentiation (LTP), known to evoke synaptic plasticity, or long-term depolarization block by KCl, leading to homeostatic morphological changes, we show that actin stabilization needed for the enlargement of dendritic spines is dependent on PKD activity. Consequently, impaired PKD functions attenuate activity-dependent changes in hippocampal dendritic spines, including LTP formation, cause morphological alterations in vivo, and have deleterious consequences on spatial memory formation. We thus provide compelling evidence that PKD controls synaptic plasticity and learning by regulating actin stability in dendritic spines.

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