scholarly journals Phospholipase D and retromer promote recycling of TRPL ion channel via the endoplasmic reticulum

Traffic ◽  
2021 ◽  
Author(s):  
Krystina Wagner ◽  
Thomas K. Smylla ◽  
Marko Lampe ◽  
Jana Krieg ◽  
Armin Huber
Keyword(s):  
Endoplasmic Reticulum ◽  
Ion Channel ◽  
Phospholipase D

scholarly journals Sympathetic storm aggravate abnormal Kv4.2 ion channel membrane transposition in rat cardiomyocytes through endoplasmic reticulum stress

Heart ◽  
2011 ◽  
Vol 97 (Suppl 3) ◽  
pp. A19-A20
Author(s):  
Z. Xiaozhen ◽  
G. Min ◽  
W. Xuehui ◽  
Z. Yong ◽  
Z. Ting ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Ion Channel ◽  
Rat Cardiomyocytes ◽  
Sympathetic Storm

Arfaptin 1, an ARF-binding protein, inhibits phospholipase D and endoplasmic reticulum/Golgi protein transport

FEBS Letters ◽  
1999 ◽  
Vol 443 (2) ◽  
pp. 197-200 ◽  
Author(s):  
Ben-Tsion Williger ◽  
Joachim Ostermann ◽  
J.H. Exton
Keyword(s):  
Endoplasmic Reticulum ◽  
Phospholipase D ◽  
Protein Transport ◽  
Binding Protein ◽  
Golgi Protein

scholarly journals Intracellular cleavage of glycosylphosphatidylinositol by phospholipase D induces activation of protein kinase Cα

1999 ◽  
Vol 342 (2) ◽  
pp. 449-455 ◽  
Author(s):  
Hiroshi TSUJIOKA ◽  
Noboru TAKAMI ◽  
Yoshio MISUMI ◽  
Yukio IKEHARA
Keyword(s):  
Signal Transduction ◽  
Endoplasmic Reticulum ◽  
Protein Kinase ◽  
Phospholipase D ◽  
Secretory Pathway ◽  
Gradient Centrifugation ◽  
Endoplasmic Reticulum Membrane ◽  
Gpi Anchor ◽  
Protein Kinase Cα ◽  
In Cells

Many proteins are anchored to the cell membrane by glycosylphosphatidylinositol (GPI). One of the functions proposed for the GPI anchor is as a possible mediator in signal transduction through its hydrolysis. GPI-specific phospholipase D (GPI-PLD) is a secretory protein that is suggested to be involved in the release of GPI-anchored protein from the membrane. In the present study we examined how GPI-PLD is involved in signal transduction. When introduced exogenously and overexpressed in cells, GPI-PLD cleaved the GPI anchors in the early secretory pathway, possibly in the endoplasmic reticulum, resulting in an increased production of diacylglycerol. Experiments in vitro and in vivo showed that the association of protein kinase Cα (PKCα) with membranes was increased markedly by expression of GPI-PLD in cells. Furthermore, sucrose-density-gradient centrifugation and immunofluorescence microscopy demonstrated that PKCα was translocated to the endoplasmic reticulum membrane in cells expressing GPI-PLD, in contrast with its association with the plasma membrane in cells treated with PMA. We also confirmed that the phosphorylation of c-Fos as well as PKCα itself was greatly enhanced by the expression of GPI-PLD. Taken together, these results suggest that GPI-PLD is involved in intracellular cleavage of the GPI anchor, which is a new potential source of diacylglycerol production to activate PKCα.

scholarly journals Phorbol ester-sensitive phospholipase D is mainly localized in the endoplasmic reticulum of BHK cells

1996 ◽  
Vol 320 (3) ◽  
pp. 885-890 ◽  
Author(s):  
Christina DECKER ◽  
Maria Jesus MIRO OBRADORS ◽  
Daniel J. SILLENCE ◽  
David ALLAN
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Phospholipase D ◽  
Phorbol Ester ◽  
Membrane Vesicles ◽  
Sucrose Density Gradient ◽  
Subcellular Fractionation ◽  
Plasma Membrane Vesicles ◽  
Intact Cells ◽  
Site Of Action

The localization of phorbol ester-sensitive phospholipase D (PLD) in baby hamster kidney cells has been investigated by determining the subcellular distribution of the phosphatidylbutanol produced when the cells are incubated with phorbol 12-myristate 13-acetate and n-butanol. Results derived by isolation of plasma membrane vesicles from intact cells or by subcellular fractionation on a sucrose density gradient suggest the PLD is specific for phosphatidylcholine and its primary site of action is not the plasma membrane but the endoplasmic reticulum.

scholarly journals Hepatitis E virus ORF3 is a functional ion channel required for release of infectious particles

2017 ◽  
Vol 114 (5) ◽  
pp. 1147-1152 ◽  
Author(s):  
Qiang Ding ◽  
Brigitte Heller ◽  
Juan M. V. Capuccino ◽  
Bokai Song ◽  
Ila Nimgaonkar ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Ion Channel ◽  
Influenza A ◽  
Hepatitis E Virus ◽  
Ionic Currents ◽  
Hepatitis E ◽  
Structural Features ◽  
Channel Activity ◽  
Direct Acting Antivirals ◽  
Direct Acting

Hepatitis E virus (HEV) is the leading cause of enterically transmitted viral hepatitis globally. Of HEV’s three ORFs, the function of ORF3 has remained elusive. Here, we demonstrate that via homophilic interactions ORF3 forms multimeric complexes associated with intracellular endoplasmic reticulum (ER)-derived membranes. HEV ORF3 shares several structural features with class I viroporins, and the function of HEV ORF3 can be maintained by replacing it with the well-characterized viroporin influenza A virus (IAV) matrix-2 protein. ORF3’s ion channel function is further evidenced by its ability to mediate ionic currents when expressed inXenopus laevisoocytes. Furthermore, we identified several positions in ORF3 critical for its formation of multimeric complexes, ion channel activity, and, ultimately, release of infectious particles. Collectively, our data demonstrate a previously undescribed function of HEV ORF3 as a viroporin, which may serve as an attractive target in developing direct-acting antivirals.

Colonic epithelium-enriched protein A4 is a proteolipid that exhibits ion channel characteristics

1997 ◽  
Vol 272 (3) ◽  
pp. C957-C965 ◽  
Author(s):  
G. E. Breitwieser ◽  
J. C. McLenithan ◽  
J. F. Cortese ◽  
J. M. Shields ◽  
M. M. Oliva ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Ion Channel ◽  
Colonic Epithelium ◽  
Xenopus Laevis Oocytes ◽  
Alpha Helices ◽  
Reading Frame ◽  
Electrophysiological Studies ◽  
Membrane Spanning

Expression of the human gene A4 is enriched in the colonic epithelium and is transcriptionally activated on differentiation of colonic epithelial cells in vitro (M. M. Oliva, T. C. Wu, and V. W. Yang. Arch. Biochem. Biophys. 302: 183-192, 1993). A4 cDNA contains an open reading frame that predicts a polypeptide of 17 kDa. To determine the function of the A4 protein, we characterized its biochemical and physiological properties. Hydropathy analysis of deduced A4 amino acid sequence revealed four putative membrane-spanning alpha-helices. The hydrophobic nature of A4 was confirmed by its being extractable with organic solvents. Immunocytochemical studies of cells expressing A4 localized it to the endoplasmic reticulum. Moreover, A4 multimerized in vivo as determined by coimmunoprecipitation experiments. The four-transmembrane topology and biophysical characteristics of A4 suggest that it belongs to a family of integral membrane proteins called proteolipids, some of which multimerize to form ion channels. Subsequent electrophysiological studies of nuclei isolated from microinjected Xenopus laevis oocytes transiently expressing A4 showed the appearance of a 28-pS channel. Thus our studies indicate that A4 is a colonic epithelium-enriched protein localized to the endoplasmic reticulum and that, similar to other proteolipids, A4 multimerizes and exhibits characteristics of an ion channel.

scholarly journals Acid-Sensing Ion Channel 1a Regulates Fate of Rat Nucleus Pulposus Cells in Acid Stimulus Through Endoplasmic Reticulum Stress

2018 ◽  
Vol 7 (1) ◽  
pp. 2-9 ◽  
Author(s):  
Zhi-Yang Xie ◽  
Lu Chen ◽  
Cong Zhang ◽  
Lei Liu ◽  
Feng Wang ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Ion Channel ◽  
Nucleus Pulposus ◽  
Nucleus Pulposus Cells
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