PLCG1 (Phospholipase C, Gamma 1)

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Phospholipase C gamma 1 (PLCG1) R707Q mutation is counterselected under targeted therapy in a patient with hepatic angiosarcoma

Hepatic angiosarcoma is a rare and aggressive vascular neoplasm. Pathogenic driver mutations are largely unknown. We present the case of a patient with recurrent hepatic angiosarcoma, who initially showed good response to sunitinib, followed by progression. Using comprehensive molecular techniques, we explored the potential mechanisms of resistance. By low-read-depth whole-genome sequencing, th...

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PLCG1 regulates USP1 phosphorylation Phospholipase C Gamma 1 Connects the Cell Membrane Pathway to the Nuclear Receptor Pathway in Insect Steroid Hormone Signaling

In addition to the classical nuclear receptor pathway, there is a non-genomic pathway in the cell membrane that regulates gene expression in animal steroid hormone signaling; however, this mechanism is unclear. Here, we report that the insect steroid hormone 20-hydroxyecdysone (20E) regulates calcium influx via phospholipase C gamma 1 (PLCG1) to modulate the protein kinase C (PKC) phosphorylati...

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Stimulation of Fc gamma RIIIA results in phospholipase C-gamma 1 tyrosine phosphorylation and p56lck activation

Binding of ligand to the alpha subunit of Fc gamma RIIIA(CD16), expressed at the natural killer (NK) cell membrane in association with homo or heterodimers of proteins of the zeta family, results in phosphorylation of several proteins on tyrosine residues. We have analyzed the role of protein tyrosine phosphorylation in the regulation of molecular events induced upon stimulation of Fc gamma RII...

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Phospholipase C-gamma 1 binds to actin-cytoskeleton via its C-terminal SH2 domain in vitro.

Association of phospholipase C (PLC)-gamma 1 with the cytoskeleton has been postulated to be one of the crucial steps for PLC-gamma 1 activation and translocation to the plasma membrane. In this report, direct binding assays were carried out to study which fragment of PLC-gamma 1 Src homology region has been able to bind to the actin-cytoskeleton. Using GST fusion proteins containing various de...

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Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.

The lipase activity of most phospholipases C (PLCs) is basally repressed by a highly degenerate and mostly disordered X/Y linker inserted within the catalytic domain. Release of this auto-inhibition is driven by electrostatic repulsion between the plasma membrane and the electronegative X/Y linker. In contrast, PLC-γ isozymes (PLC-γ1 and -γ2) are structurally distinct from other PLCs because mu...

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ژورنال

عنوان ژورنال: Atlas of Genetics and Cytogenetics in Oncology and Haematology

سال: 2014

ISSN: 1768-3262

DOI: 10.4267/2042/54035