scholarly journals Role of protein kinase D (PKD) phosphorylation of Oxysterol binding protein (OSBP) in sphingomyelin biosynthesis

2011 ◽  
Vol 25 (S1) ◽  
Author(s):  
Asako Goto ◽  
Neale Ridgway
Keyword(s):  
Protein Kinase ◽  
Binding Protein ◽  
Protein Kinase D ◽  
Oxysterol Binding Protein

scholarly journals Regulation of Oxysterol-binding Protein Golgi Localization through Protein Kinase D–mediated Phosphorylation

2010 ◽  
Vol 21 (13) ◽  
pp. 2327-2337 ◽  
Author(s):  
Sokha Nhek ◽  
Mike Ngo ◽  
Xuemei Yang ◽  
Michelle M. Ng ◽  
Seth J. Field ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Binding Protein ◽  
Critical Role ◽  
Protein Kinase D ◽  
Cholesterol Depletion ◽  
Oxysterol Binding Protein ◽  
Golgi Localization ◽  
Golgi Network

Protein kinase D (PKD) plays a critical role at the trans-Golgi network by regulating the fission of transport carriers destined for the plasma membrane. Two known Golgi-localized PKD substrates, PI4-kinase IIIβ and the ceramide transfer protein CERT, mediate PKD signaling to influence vesicle trafficking to the plasma membrane and sphingomyelin synthesis, respectively. PKD is recruited and activated at the Golgi through interaction with diacylglycerol, a pool of which is generated as a by-product of sphingomyelin synthesis from ceramide. Here we identify a novel substrate of PKD at the Golgi, the oxysterol-binding protein OSBP. Using a substrate-directed phospho-specific antibody that recognizes the optimal PKD consensus motif, we show that PKD phosphorylates OSBP at Ser240 in vitro and in cells. We further show that OSBP phosphorylation occurs at the Golgi. Phosphorylation of OSBP by PKD does not modulate dimerization, sterol binding, or affinity for PI(4)P. Instead, phosphorylation attenuates OSBP Golgi localization in response to 25-hydroxycholesterol and cholesterol depletion, impairs CERT Golgi localization, and promotes Golgi fragmentation.

scholarly journals Critical role of X-box binding protein 1 in NADPH oxidase 4-triggered cardiac hypertrophy is mediated by receptor interacting protein kinase 1

Cell Cycle ◽  
2017 ◽  
Vol 16 (4) ◽  
pp. 348-359 ◽  
Author(s):  
Li Chen ◽  
Mingyue Zhao ◽  
Junli Li ◽  
Yu Wang ◽  
Qinxue Bao ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Nadph Oxidase ◽  
Cardiac Hypertrophy ◽  
Binding Protein ◽  
Critical Role ◽  
Interacting Protein ◽  
Nadph Oxidase 4

The role of protein kinase C-δ in PTH stimulation of IGF-binding protein-5 mRNA in UMR-106–01 cells

2002 ◽  
Vol 282 (3) ◽  
pp. E534-E541 ◽  
Author(s):  
Mary S. Erclik ◽  
Jane Mitchell
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Binding Protein ◽  
Specific Inhibitor ◽  
Dominant Negative Mutant ◽  
Nuclear Fraction ◽  
Mrna Levels ◽  
Kinase C ◽  
Umr 106

We have investigated the role of protein kinase C (PKC) signal transduction pathways in parathyroid hormone (PTH) regulation of insulin-like growth factor-binding protein-5 (IGFBP-5) gene expression in the rat osteoblast-like cell line UMR-106–01. Involvement of the PKC pathway was determined by the findings that bisindolylmaleimide I inhibited 40% of the PTH effect, and 1 μM bovine PTH-(3–34) stimulated a 10-fold induction of IGFBP-5 mRNA. PTH-(1–34) and PTH-(3–34) (100 nM) both stimulated PKC-δ translocation from the membrane to the nuclear fraction. Rottlerin, a PKC-δ-specific inhibitor, and a dominant negative mutant of PKC-δ were both able to significantly inhibit PTH-(1–34) and PTH-(3–34) induction of IGFBP-5 mRNA, suggesting a stimulatory role for PKC-δ in the effects of PTH. Phorbol 12-myristate 13-acetate (PMA) stimulated PKC-α translocation from the cytosol to the membrane and inhibited ∼50% of the PTH-(1–34), forskolin, and 8-bromoadenosine 3′,5′-cyclic monophosphate-stimulated IGFBP-5 mRNA levels, suggesting that PKC-α negatively regulates protein kinase A (PKA)-mediated induction of IGFBP-5 mRNA. These results suggest that the induction of IGFBP-5 by PTH is both PKA and PKC dependent and PKC-δ is the primary mediator of the effects of PTH via the PKC pathway.

scholarly journals The Role of Protein Kinase C in the Transient Association of p57, a Coronin Family Actin-Binding Protein, with Phagosomes

2002 ◽  
Vol 25 (7) ◽  
pp. 837-844 ◽  
Author(s):  
Saotomo Itoh ◽  
Kensuke Suzuki ◽  
Jun Nishihata ◽  
Mitsusada Iwasa ◽  
Teruaki Oku ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Binding Protein ◽  
Actin Binding ◽  
Actin Binding Protein ◽  
Kinase C

scholarly journals Critical role of protein kinase D in VEGF‐induced vascular permeability and angiogenesis

2015 ◽  
Vol 29 (S1) ◽  
Author(s):  
Zheng Gen Jin ◽  
Jinjing Zhao ◽  
Meimei Yin ◽  
Il‐Sun Kwon ◽  
Michael Mastrangelo
Keyword(s):  
Protein Kinase ◽  
Vascular Permeability ◽  
Critical Role ◽  
Protein Kinase D

Impaired insulin exocytosis in chronic hepatitis C infection: contributory role of p38δ MAPK–protein kinase D–golgi complex axis

2020 ◽  
Vol 134 (12) ◽  
pp. 1449-1456
Author(s):  
Parimala Narne
Keyword(s):  
Hepatitis C ◽  
Protein Kinase ◽  
Golgi Complex ◽  
Hcv Infection ◽  
Protein Kinase D ◽  
Cell Dysfunction ◽  
Chronic Hcv Infection ◽  
Chronic Hcv ◽  
Insulin Exocytosis

Abstract Hepatitis C virus (HCV) infection and chronic hepatitis C (CHC) are associated with a measurable risk of insulin resistance (IR)/impaired glucose tolerance (IGT)/diabetes mellitus (DM). While loss of hepatic endocrine function contributes to liver cirrhosis in diabetic patients, onset and progression of IR/IGT to diabetes and exacerbation of incident hyperglycemia are ostensibly linked with chronic HCV infection. In this regard, the study by Chen J et al. appearing in Clinical Science (2020) (134(5) https://doi.org/10.1042/CS20190900) attempts to understand the mechanisms underlying the savaging effects of chronic HCV infection on insulin-producing pancreatic β-cells and hence diabetic onset. The study investigated the role of mitogen-activated protein kinase (MAPK) p38δ–protein kinase D (PKD)–golgi complex axis in impacting insulin exocytosis. It was inferred that an insulin secretory defect of pancreatic β-cells, owing to disrupted insulin exocytosis, to an extent explains β-cell dysfunction in HCV-infected or CHC milieu. HCV infection negatively regulates first-phase and second-phase insulin secretion by impinging on PKD-dependent insulin secretory granule fission at trans-golgi network and insulin secretory vesicle membrane fusion events. This commentary highlights the study in question, that deciphered the contribution of p38δ MAPK–PKD–golgi complex axis to β-cell dysfunction in CHC milieu. This pivotal axis proffers a formidable therapeutic opportunity for alleviation of double burden of glucose abnormalities/DM and CHC.

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