Dataset Information

Human Protein Tyrosine Phosphatase Interaction Network

ABSTRACT: As the remarkable prevalence of activated protein tyrosine kinases (TKs) as oncoproteins and their mutations being identified in numerous cancers, the control of protein tyrosine phosphorylation has been considered to play a central role in ensuring the homeostasis of cellular physiology and thus, preventing tumorigenesis. Protein tyrosine phosphatases (PTPs) can contribute to this equilibrium of protein tyrosine phosphorylation and thereby antagonize the oncogenic activities of tyrosine kinases, therefore, PTPs are prominently considered to act as tumor suppressors. To achieve a comprehensive understanding of the protein-protein interaction network for this PTP family, we isolated the ~ 70 PTP-associated protein complexes from HEK293T cells and provided a systematically proteomic analysis for this tumor suppressor family.

INSTRUMENT(S): LTQ Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Hek-293t Cell, Early Embryonic Cell

SUBMITTER: Xu Li

LAB HEAD: Junjie Chen

PROVIDER: PXD002462 | Pride | 2016-08-17

REPOSITORIES: Pride

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Defining the Protein-Protein Interaction Network of the Human Protein Tyrosine Phosphatase Family.

Li Xu X Tran Kim My KM Aziz Kathryn E KE Sorokin Alexey V AV Chen Junjie J Wang Wenqi W

Molecular & cellular proteomics : MCP 20160718 9

Protein tyrosine phosphorylation, which plays a vital role in a variety of human cellular processes, is coordinated by protein tyrosine kinases and protein tyrosine phosphatases (PTPs). Genomic studies provide compelling evidence that PTPs are frequently mutated in various human cancers, suggesting that they have important roles in tumor suppression. However, the cellular functions and regulatory machineries of most PTPs are still largely unknown. To gain a comprehensive understanding of the pro ...[more]

PMID: 27432908

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Project description:Although the consequences of genotoxic injury include cell cycle arrest and apoptosis, cell survival responses after genotoxic injury can produce intrinsic death-resistance and contribute to the development of a transformed phenotype. Protein tyrosine phosphatases (PTPs) are integral components of key survival pathways, and are responsible for their inactivation, while PTP inhibition is are often associated with enhanced cell proliferation. Our aim was to elucidate signaling events that modulate cell survival after genotoxin exposure. Diploid human lung fibroblasts (HLF) were treated with Cr(VI) (as Na2CrO4), a well known human respiratory carcinogen that induces a wide spectrum of DNA damage, in the presence and absence of a broad-range PTP inhibitor, sodium orthovanadate. Notably, PTP inhibition abrogated Cr(VI)-induced clonogenic lethality. The enhanced survival of Cr(VI)-exposed cells after PTP inhibition was predominantly due to a bypass of cell cycle arrest and was not due to decreased Cr uptake as evidenced by unchanged Cr-DNA adduct burden. Additionally, the bypass of Cr-induced growth arrest by PTP inhibition, was accompanied by a decrease in Cr(VI)-induced expression of cell cycle inhibiting genes, and an increase in the Cr(VI)-induced expression of cell cycle promoting genes. Importantly, PTP inhibition resulted in an increase in forward mutations at the HPRT locus, supporting the hypothesis that PTP inhibition in the presence of DNA damage may lead to genomic instability, via bypass of cell cycle checkpoints. Experiment Overall Design: Experimental factor was chemical treatment type (3 of them) Experiment Overall Design: (1) No: HLF 1-1, HLF 1-2, HLF 1-3, HLF 1-4 Experiment Overall Design: (2) 1uM Cr(VI): HLF 3-1, HLF 3-2, HLF 3-3, HLF 3-4 Experiment Overall Design: (3) 10uM SOV + 1uM Cr(VI): HLF 4-1, HLF 4-2, HLF 4-3, HLF 4-4 Experiment Overall Design: Biological replicates: 4 different RNA extractions from 4 different cell cultures=quadruplicate per chemical treatment type

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