Protein Phosphorylation and Cell Signaling Series II

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cell Signaling".

Deadline for manuscript submissions: closed (20 November 2022) | Viewed by 2965

Special Issue Editor

Special Issue Information

Dear Colleagues,

Phosphorylation is one of the most important and most commonly occurring posttranslational modifications of proteins. Protein phosphorylation plays a critical role in cell signaling in response to extracellular stimulus and is of fundamental importance in biological regulation.

Protein phosphorylation is controlled by protein kinases and protein phosphatases. A protein kinase is a kinase enzyme that modifies other molecules, mostly proteins, by chemically adding phosphate groups to them (phosphorylation). The human genome contains about 518 protein kinase genes, and they constitute about 2% of all human genes. A protein could be phosphorylated in three amino acids, including tyrosine (Tyr, Y), Serine (Ser, S), and Threonine (Thr, T). A protein phosphatase is a phosphatase enzyme that removes a phosphate group from the phosphorylated amino acid residue of its substrate protein. While there are 107 genes in the human genome that encode protein tyrosine phosphatase, there are only a few serine/threonine phosphatases.

Up to 30% of all human proteins may be modified by protein kinase and phosphatase. Phosphorylation and de-phosphorylation commonly act as a switch to turn on and off a signaling cascade. Protein phosphorylation usually results in a functional change of the target protein (substrate) by changing enzyme activity, cellular location, or association with other proteins, which frequently lead to the changes in the biological function of the cell.

This Special Issue will cover the recent progress in all of the areas related to protein phosphorylation and cell signaling. Both original research articles and reviews are welcome.

Prof. Zhixiang Wang
Guest Editor

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Keywords

  • protein phosphorylation
  • proein de-phosphorylation
  • protein kinases
  • protein phosphatases
  • tyrosine kinases
  • receptor tyrosine kinases
  • serine/threonin kinases
  • tyrosine phosphatases
  • serine/threonin phosphatases
  • extracellular stimulus
  • cell signaling
  • signal transduction
  • structures
  • functions

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Published Papers (1 paper)

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Research

22 pages, 3025 KiB  
Article
Proteomics and Phospho-Proteomics Profiling of the Co-Formulation of Type I and II Interferons, HeberFERON, in the Glioblastoma-Derived Cell Line U-87 MG
by Dania Vázquez-Blomquist, Anette Hardy-Sosa, Saiyet C. Baez, Vladimir Besada, Sucel Palomares, Osmany Guirola, Yassel Ramos, Jacek R. Wiśniewski, Luis Javier González and Iraldo Bello-Rivero
Cells 2022, 11(24), 4068; https://doi.org/10.3390/cells11244068 - 15 Dec 2022
Cited by 2 | Viewed by 2113
Abstract
HeberFERON, a co-formulation of Interferon (IFN)-α2b and IFN-γ, has effects on skin cancer and other solid tumors. It has antiproliferative effects over glioblastoma multiform (GBM) clones and cultured cell lines, including U-87 MG. Here, we report the first label-free quantitative proteomic and phospho-proteomic [...] Read more.
HeberFERON, a co-formulation of Interferon (IFN)-α2b and IFN-γ, has effects on skin cancer and other solid tumors. It has antiproliferative effects over glioblastoma multiform (GBM) clones and cultured cell lines, including U-87 MG. Here, we report the first label-free quantitative proteomic and phospho-proteomic analyses to evaluate changes induced by HeberFERON after 72 h incubation of U-87 MG that can explain the effect on cellular proliferation. LC-MS/MS, functional enrichment and networking analysis were performed. We identified 7627 proteins; 122 and 211 were down- and up-regulated by HeberFERON (fold change > 2; p < 0.05), respectively. We identified 23,549 peptides (5692 proteins) and 8900 phospho-peptides; 523 of these phospho-peptides (359 proteins) were differentially modified. Proteomic enrichment showed IFN signaling and its control, direct and indirect antiviral mechanisms were the main modulated processes. Phospho-proteome enrichment displayed the cell cycle as one of the most commonly targeted events together with cytoskeleton organization; translation/RNA splicing, autophagy and DNA repair, as represented biological processes. There is a high interconnection of phosphoproteins in a molecular network; mTOR occupies a centric hub with interactions with translation machinery, cytoskeleton and autophagy components. Novel phosphosites and others with unknown biological functionality in key players in the aforementioned processes were regulated by HeberFERON and involved CDK and ERK kinases. These findings open new experimental hypotheses regarding HeberFERON action. The results obtained contribute to a better understanding of HeberFERON effector mechanisms in the context of GBM treatment. Full article
(This article belongs to the Special Issue Protein Phosphorylation and Cell Signaling Series II)
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