The molecular mechanism of acylation stimulating protein regulation of adipophilin and perilipin expression: Involvement of phosphoinositide 3-kinase and phospholipase C

2011 ◽  
Vol 112 (6) ◽  
pp. 1622-1629 ◽  
Author(s):  
Jing WU ◽  
Zhou-Yang JIAO ◽  
Hui-Ling LU ◽  
Jing Zhang ◽  
Han-Hua Lin ◽  
...  
Keyword(s):  
Phospholipase C ◽  
Molecular Mechanism ◽  
Protein Regulation ◽  
Acylation Stimulating Protein ◽  
Phosphoinositide 3 Kinase

scholarly journals Progesterone-Dependent Induction of Phospholipase C-Related Catalytically Inactive Protein 1 (PRIP-1) in Decidualizing Human Endometrial Stromal Cells

Endocrinology ◽  
2016 ◽  
Vol 157 (7) ◽  
pp. 2883-2893 ◽  
Author(s):  
Joanne Muter ◽  
Paul J. Brighton ◽  
Emma S. Lucas ◽  
Lauren Lacey ◽  
Anatoly Shmygol ◽  
...  
Keyword(s):  
Phospholipase C ◽  
Stromal Cells ◽  
Nuclear Translocation ◽  
Scaffold Protein ◽  
Trophoblast Invasion ◽  
Differentiation Markers ◽  
Endometrial Stromal Cells ◽  
Decidual Cells ◽  
Phosphoinositide 3 Kinase ◽  
Inactive Protein

Decidualization denotes the transformation of endometrial stromal cells into specialized decidual cells. In pregnancy, decidual cells form a protective matrix around the implanting embryo, enabling coordinated trophoblast invasion and formation of a functional placenta. Continuous progesterone (P4) signaling renders decidual cells resistant to various environmental stressors, whereas withdrawal inevitably triggers tissue breakdown and menstruation or miscarriage. Here, we show that PLCL1, coding phospholipase C (PLC)-related catalytically inactive protein 1 (PRIP-1), is highly induced in response to P4 signaling in decidualizing human endometrial stromal cells (HESCs). Knockdown experiments in undifferentiated HESCs revealed that PRIP-1 maintains basal phosphoinositide 3-kinase/Protein kinase B activity, which in turn prevents illicit nuclear translocation of the transcription factor forkhead box protein O1 and induction of the apoptotic activator BIM. By contrast, loss of this scaffold protein did not compromise survival of decidual cells. PRIP-1 knockdown did also not interfere with the responsiveness of HESCs to deciduogenic cues, although the overall expression of differentiation markers, such as PRL, IGFBP1, and WNT4, was blunted. Finally, we show that PRIP-1 in decidual cells uncouples PLC activation from intracellular Ca2+ release by attenuating inositol 1,4,5-trisphosphate signaling. In summary, PRIP-1 is a multifaceted P4-inducible scaffold protein that gates the activity of major signal transduction pathways in the endometrium. It prevents apoptosis of proliferating stromal cells and contributes to the relative autonomy of decidual cells by silencing PLC signaling downstream of Gq protein-coupled receptors.

G-protein regulation of a soluble phospholipase C in HL-60 granulocytes

1990 ◽  
Vol 14 ◽  
pp. 10
Author(s):  
P GIERSCHIK ◽  
M CAMPS ◽  
C HOU ◽  
E STROHMAIER ◽  
S GIERSCHIK
Keyword(s):  
Phospholipase C ◽  
G Protein ◽  
Protein Regulation

G-Protein Regulation of Phospholipase C in the Turkey Erythrocyte

1993 ◽  
pp. 401-415
Author(s):  
A. J. Morris ◽  
D. H. Maurice ◽  
G. L. Waldo ◽  
J. L. Boyer ◽  
T. K. Harden
Keyword(s):  
Phospholipase C ◽  
G Protein ◽  
Protein Regulation

scholarly journals Vav1 Transduces T Cell Receptor Signals to the Activation of Phospholipase C-γ1 via Phosphoinositide 3-Kinase-dependent and -independent Pathways

2002 ◽  
Vol 195 (9) ◽  
pp. 1103-1114 ◽  
Author(s):  
Lucinda F. Reynolds ◽  
Lesley A. Smyth ◽  
Trisha Norton ◽  
Norman Freshney ◽  
Julian Downward ◽  
...  
Keyword(s):  
T Cell ◽  
Phospholipase C ◽  
T Cell Receptor ◽  
Genetic System ◽  
Cell Receptor ◽  
Calcium Flux ◽  
Double Positive ◽  
Signaling Complex ◽  
Tcr Signals ◽  
Phosphoinositide 3 Kinase

Vav1 is a signal transducing protein required for T cell receptor (TCR) signals that drive positive and negative selection in the thymus. Furthermore, Vav1-deficient thymocytes show greatly reduced TCR-induced intracellular calcium flux. Using a novel genetic system which allows the study of signaling in highly enriched populations of CD4+CD8+ double positive thymocytes, we have studied the mechanism by which Vav1 regulates TCR-induced calcium flux. We show that in Vav1-deficient double positive thymocytes, phosphorylation, and activation of phospholipase C-γ1 (PLCγ1) is defective. Furthermore, we demonstrate that Vav1 regulates PLCγ1 phosphorylation by at least two distinct pathways. First, in the absence of Vav1 the Tec-family kinases Itk and Tec are no longer activated, most likely as a result of a defect in phosphoinositide 3-kinase (PI3K) activation. Second, Vav1-deficient thymocytes show defective assembly of a signaling complex containing PLCγ1 and the adaptor molecule Src homology 2 domain–containing leukocyte phosphoprotein 76. We show that this latter function is independent of PI3K.

Cross-talk between phospholipase C and phosphoinositide 3-kinase signalling pathways

1997 ◽  
Vol 25 (4) ◽  
pp. 1132-1137 ◽  
Author(s):  
I. H. Batty ◽  
D. M. Hickinson ◽  
C. P. Dowries
Keyword(s):  
Phospholipase C ◽  
Cross Talk ◽  
Signalling Pathways ◽  
Phosphoinositide 3 Kinase

Phosphoinositide 3-kinase-dependent regulation of phospholipase Cγ

2007 ◽  
Vol 35 (2) ◽  
pp. 229-230 ◽  
Author(s):  
T. Maffucci ◽  
M. Falasca
Keyword(s):  
Phospholipase C ◽  
Tyrosine Kinases ◽  
Receptor Tyrosine Kinases ◽  
Second Messengers ◽  
Pleckstrin Homology Domain ◽  
Ph Domain ◽  
Pleckstrin Homology ◽  
Functional Roles ◽  
Phosphoinositide 3 Kinase

Activation of the enzyme PLC (phospholipase C) leads to the formation of second messengers Ins(1,4,5)P3 and diacylglycerol. RTKs (receptor tyrosine kinases) activate this reaction through PLCγ isoenzymes. It has been shown that PI3K (phosphoinositide 3-kinase) may regulate PLCγ activity through the interaction of PI3K product PtdIns(3,4,5)P3 and the PLCγ PH domain (pleckstrin homology domain). Here, we analyse the potential functional roles of the PI3K/PLC pathway.

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