Proteomics

Dataset Information

0

Global post-translational modification profiling of HIV-1-infected cells reveals mechanisms of host cellular pathway remodeling


ABSTRACT: Viruses must effectively remodel host cellular pathways to replicate and evade immune defenses, and they must do so with limited genomic coding capacity. Targeting post-translational modification (PTM) pathways provides a mechanism by which viruses can broadly and rapidly transform a hostile host environment into a hospitable one. We used mass spectrometry-based proteomics to quantify changes in protein abundance and two PTM types – phosphorylation and ubiquitination – in response to HIV-1 infection with viruses harboring targeted deletions of a subset of HIV-1 genes. PTM analysis revealed a requirement for Aurora kinase activity in HIV-1 infection and identified substrates of a phosphatase that is degraded during infection. Finally, we demonstrated that the Cullin4A-DDB1-DCAF1 E3 ubiquitin ligase ubiquitinates histone H1 somatic isoforms and that the HIV-1 Vpr protein inhibits this process, leading to defects in DNA repair.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Kidney

DISEASE(S): Human Immunodeficiency Virus Infectious Disease

SUBMITTER: Jeffrey Johnson  

LAB HEAD: Jeffrey Johnson

PROVIDER: PXD032085 | Pride | 2022-04-14

REPOSITORIES: Pride

Dataset's files

Source:
altmetric image

Publications


Viruses must effectively remodel host cellular pathways to replicate and evade immune defenses, and they must do so with limited genomic coding capacity. Targeting post-translational modification (PTM) pathways provides a mechanism by which viruses can broadly and rapidly transform a hostile host environment into a hospitable one. We use mass spectrometry-based proteomics to quantify changes in protein abundance and two PTM types-phosphorylation and ubiquitination-in response to HIV-1 infection  ...[more]

Similar Datasets

2019-06-24 | GSE126594 | GEO
2023-11-13 | PXD038655 | Pride
2023-02-17 | PXD035557 | Pride
2022-10-01 | PXD033763 | Pride
2023-03-11 | PXD030816 | Pride
2021-07-16 | GSE180044 | GEO
2018-06-06 | MTBLS449 | MetaboLights
2008-10-02 | GSE12963 | GEO
2023-06-14 | PXD040496 | Pride
2008-10-26 | E-GEOD-12963 | biostudies-arrayexpress