Proteomics

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Quantitative proteomics and phosphoproteomics reveal that PIM3 modulates cell migration via regulating Rho GTPase signaling


ABSTRACT: Stable cell line was used for this study, so there are minimum variations between samples. For the lable free based quantitative analysis of the whole proteome, three biological replicates for each condition were investigated. For the phosphoproteomic analysis, three biological replicates and two technical replicates were analyzed, resulting in twelve data for quantification. Statistical analysis was performed using student’s t-test

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Na Jiang  

LAB HEAD: Ruibing Chen

PROVIDER: PXD014045 | Pride | 2020-02-04

REPOSITORIES: Pride

Dataset's files

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Action DRS
OFL000228-PCDH1-F1.raw Raw
OFL000229-PCDH1-F2.raw Raw
OFL000230-PCDH1-F3.raw Raw
OFL000231-PCDH1-F4.raw Raw
OFL000232-PCDH2-F1.raw Raw
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Publications

Proto-Oncogene Serine/Threonine Kinase PIM3 Promotes Cell Migration via Modulating Rho GTPase Signaling.

Dang Yamei Y   Jiang Na N   Wang Hao H   Chen Xuechun X   Gao Yan Y   Zhang Xiangyang X   Qin Guoxuan G   Li Yongmei Y   Chen Ruibing R  

Journal of proteome research 20200207 3


The proto-oncogene serine/threonine-protein kinase PIM3 plays critical roles in cancer, and it has been extensively exploited as a drug target. Here, we investigated the quantitative changes in the cellular proteome and phosphoproteome in liver cancer cells overexpressing PIM3 to obtain a better understanding of the regulatory functions of PIM3 and the underlying molecular mechanisms. This work depicted the landscape of gene expression and protein phosphorylation potentially regulated by PIM3. A  ...[more]

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