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The Importance of Tyrosine Phosphorylation Control of Cellular Signaling Pathways in Respiratory Disease: pY and pY Not.

ABSTRACT: Reversible phosphorylation of proteins on tyrosine residues is an essential signaling mechanism by which diverse cellular processes are closely regulated. The tight temporal and spatial control of the tyrosine phosphorylation status of proteins by protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs) is critical to cellular homeostasis as well as to adaptations to the external environment. Via regulation of cellular signaling cascades involving other protein kinases and phosphatases, receptors, adaptor proteins, and transcription factors, PTKs and PTPs closely control diverse cellular processes such as proliferation, differentiation, migration, inflammation, and maintenance of cellular barrier function. Given these key regulatory roles, it is not surprising that dysfunction of PTKs and PTPs is important in the pathogenesis of human disease, including many pulmonary diseases. The roles of various PTKs and PTPs in acute lung injury and repair, pulmonary fibrosis, pulmonary vascular disease, and inflammatory airway disease are discussed in this review. It is important to note that although there is overlap among many of these proteins in various disease states, the mechanisms by which they influence the pathogenesis of these conditions differ, suggesting wide-ranging roles for these enzymes and their potential as therapeutic targets.

SUBMITTER: Aschner Y

PROVIDER: S-EPMC6236691 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature

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The Importance of Tyrosine Phosphorylation Control of Cellular Signaling Pathways in Respiratory Disease: pY and pY Not.

Aschner Yael Y Downey Gregory P GP

American journal of respiratory cell and molecular biology 20181101 5

Reversible phosphorylation of proteins on tyrosine residues is an essential signaling mechanism by which diverse cellular processes are closely regulated. The tight temporal and spatial control of the tyrosine phosphorylation status of proteins by protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs) is critical to cellular homeostasis as well as to adaptations to the external environment. Via regulation of cellular signaling cascades involving other protein kinases and phosph ...[more]

PMID: 29812954

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Project description:Protein phosphorylation, one of the most common and important modifications of acute and reversible regulation of protein function, plays a dominant role in almost all cellular processes. These signaling events regulate cellular responses, including proliferation, differentiation, metabolism, survival, and apoptosis. Several studies have been successfully used to identify phosphorylated proteins and dynamic changes in phosphorylation status after stimulation. Nevertheless, it is still rather difficult to elucidate precise complex phosphorylation signaling pathways. In particular, how signal transduction pathways directly communicate from the outer cell surface through cytoplasmic space and then directly into chromatin networks to change the transcriptional and epigenetic landscape remains poorly understood. Here, we describe the optimization and comparison of methods based on thiophosphorylation affinity enrichment, which can be utilized to monitor phosphorylation signaling into chromatin by isolation of phosphoprotein containing nucleosomes, a method we term phosphorylation-specific chromatin affinity purification (PS-ChAP). We utilized this PS-ChAP(1) approach in combination with quantitative proteomics to identify changes in the phosphorylation status of chromatin-bound proteins on nucleosomes following perturbation of transcriptional processes. We also demonstrate that this method can be employed to map phosphoprotein signaling into chromatin containing nucleosomes through identifying the genes those phosphorylated proteins are found on via thiophosphate PS-ChAP-qPCR. Thus, our results showed that PS-ChAP offers a new strategy for studying cellular signaling and chromatin biology, allowing us to directly and comprehensively investigate phosphorylation signaling into chromatin to investigate if these pathways are involved in altering gene expression. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium with the data set identifier PXD002436.

Dataset Information

The Importance of Tyrosine Phosphorylation Control of Cellular Signaling Pathways in Respiratory Disease: pY and pY Not.

Publications

The Importance of Tyrosine Phosphorylation Control of Cellular Signaling Pathways in Respiratory Disease: pY and pY Not.

Similar Datasets

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