Proteomics

Dataset Information

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Comparative interactomes of VRK1 and VRK3: implication in cell cycle, chromatin assembly, RNA processing and DNA repair

ABSTRACT: Vaccinia related kinase (VRK) family is a ser/threonine kinase. VRK1 and VRK3 are localized in the same organelle, mainly in the nucleus. Comparative interactomes of VRK1 and VRK3 were not performed yet. We identified over 200 unreported VRK1/3-interacting proteins by proteomics-based analyses using the complementary mass spectrometry approach. Among those proteins, nuclear and cytoplasmic proteins were mostly enriched reflecting nuclear and cytoplasmic localization of VRK1/3. The interaction networks of interactome indicated biological processes associated with cell cycle, DNA repair, chromatin assembly and RNA processing. Interactions and co-localization of NCL, PARP1, HSP70, XRCC5, p53, NPM1, BAF1, cyclinB1 and ALYREF with VRK1/3 were confirmed by co-immunoprecipitation and immunofluorescent staining. Overall, this study represents a valuable resource for investigating VRK1 and VRK3 functions in health and disease, encompassing emerging themes of VRK1/3 regulation in cell cycle, mRNA processing, chromatin assembly and DNA repair.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hepatocyte

SUBMITTER: Dae-Kyum Kim  

LAB HEAD: Kwan Yong Choi

PROVIDER: PXD004103 | Pride | 2018-10-26

REPOSITORIES: Pride

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Publications

Comparative Interactomes of VRK1 and VRK3 with Their Distinct Roles in the Cell Cycle of Liver Cancer.

Lee Namgyu N   Kim Dae-Kyum DK   Han Seung Hyun SH   Ryu Hye Guk HG   Park Sung Jin SJ   Kim Kyong-Tai KT   Choi Kwan Yong KY  

Molecules and cells 20170920 9

Vaccinia-related kinase 1 (VRK1) and VRK3 are members of the VRK family of serine/threonine kinases and are principally localized in the nucleus. Despite the crucial roles of VRK1/VRK3 in physiology and disease, the molecular and functional interactions of VRK1/VRK3 are poorly understood. Here, we identified over 200 unreported VRK1/VRK3-interacting candidate proteins by affinity purification and LC-MS/MS. The networks of VRK1 and VRK3 interactomes were found to be associated with important biol  ...[more]

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