Dataset Information

Characterization of the PAK4 interactome by quantitative mass spectrometry

ABSTRACT: p21-activated kinase 4 (PAK4) is a serine/threonine kinase critical during development and with a proposed role in cancer and related cellular processes, including cell proliferation, survival and migration. However, while a limited number of PAK4-interacting proteins have been identified, the PAK4 interactome has not been systematically characterized. Here, we employed iTRAQ-based quantitative mass spectrometry of PAK4-immunioprecipitations from three distinct isolated cellular fractions to comprehensively profile the PAK4 interactome in human. These data will provide a valuable resource for further investigations on the role of PAK4 in physiology and disease.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Malignant Neoplasm Of Ovary,Breast Cancer

SUBMITTER: Henrik J Johansson

LAB HEAD: Janne Lehtiö

PROVIDER: PXD004086 | Pride | 2018-10-27

REPOSITORIES: Pride

ACCESS DATA

Publications

Identification of the PAK4 interactome reveals PAK4 phosphorylation of N-WASP and promotion of Arp2/3-dependent actin polymerization.

Zhao Miao M Spiess Matthias M Johansson Henrik J HJ Olofsson Helene H Hu Jianjiang J Lehtiö Janne J Strömblad Staffan S

Oncotarget 20170818 44

p21-activated kinase 4 (PAK4) regulates cell proliferation, apoptosis, cell motility and F-actin remodeling, but the PAK4 interactome has not been systematically analyzed. Here, we comprehensively characterized the human PAK4 interactome by iTRAQ quantitative mass spectrometry of PAK4-immunoprecipitations. Consistent with its multiple reported functions, the PAK4 interactome was enriched in diverse protein networks, including the 14-3-3, proteasome, replication fork, CCT and Arp2/3 complexes. Be ...[more]

PMID: 29100370

Similar Datasets

Project description:Spermatogenesis is a complex cell differentiation process that includes marked genetic, cellular functional and structural changes. It requires tight regulation, since disturbances in any of the spermatogenic stages would lead to fertility deficiencies. In order to increase our knowledge of signal transduction during sperm development, we carried out a large-scale identification of the phosphorylation events that occur in the human gonad. Metal oxide affinity chromatography using TiOx combined with LC-MS/MS was conducted to profile the phosphoproteome of human testes with full spermatogenesis. A total of 8187 phosphopeptides derived from 2661 proteins were identified, resulting in the most complete report of human testicular phosphoproteins to date. Phosphorylation events were enriched in proteins functionally related to spermatogenesis, as well as to highly active processes in the male gonad, such as transcriptional and translational regulation, cytoskeleton organization, DNA packaging, cell cycle and apoptosis. Moreover, 174 phosphorylated kinases were identified. The most active and abundant human protein kinases in the testis were predicted both by the phosphorylation status of the kinase activation loop and the number of phosphopeptide spectra identified. The potential function of two of those kinases, cyclin-dependent kinase 12 (CDK12) and p21-activated kinase 4(PAK4), has been explored by protein-protein interaction analysis, immunodetection in human and mouse testicular tissue, and functional assay in a human embryonal carcinoma cell line. The co-localization of CDK12 with Golgi markers and probably pro-acrosomal vesicles suggests a potential crucial role of this protein kinase in sperm formation. PAK4 expression has been found limited to human spermatogonia, and a role in embryonal carcinoma cell response to apoptosis has been observed. Together, our data confirm that phosphoregulation by protein kinases is highly active in sperm differentiation, and open a window to detailed characterization and validation of potential targets for the development of drugs modulating male fertility, and tumor behavior.

Dataset Information

Characterization of the PAK4 interactome by quantitative mass spectrometry

Publications

Identification of the PAK4 interactome reveals PAK4 phosphorylation of N-WASP and promotion of Arp2/3-dependent actin polymerization.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure