A proteome-scale map of the human interactome network.

Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.

PMID:32296183

A reference map of the human binary protein interactome.

PMID:34445249

The SCF Complex Is Essential to Maintain Genome and Chromosome Stability.

Review of the SKP1-CUL1-F-box (SCF) E3 ubiquitin ligase family in which the variable F-box subunit determines substrate specificity; provides the basis for the ComplexPortal NAS annotations placing FBXO34 in an SCF complex and SCF-dependent proteasomal degradation.

PMID:36285453

FBXO34 promotes latent HIV-1 activation by post-transcriptional modulation.

FBXO34 is a substrate-recognition component of an SCF-type E3 ubiquitin ligase that promotes ubiquitination and proteasomal degradation of HNRNPU/hnRNP U; degradation of hnRNP U abolishes its interaction with HIV-1 Rev mRNA and thereby promotes latent HIV-1 activation.

file:human/FBXO34/FBXO34-deep-research-falcon.md

Falcon deep research report for human FBXO34

A genome-wide CRISPR-Cas9 activation screen identified FBXO34 as a host factor whose activation promotes latent HIV-1 reactivation, and AP-MS/co-IP identified hnRNP U as an FBXO34-interacting substrate whose ubiquitination and degradation FBXO34 promotes.

"A genome-wide **CRISPR-Cas9 activation** screen in a latent HIV model identified **FBXO34** as a host factor whose activation promotes latent HIV reactivation. The study then used **affinity purification mass spectrometry** and **co-immunoprecipitation** to identify **hnRNP U** as an FBXO34-interacting protein and presents evidence consistent with FBXO34 promoting **hnRNP U ubiquitination** and **decreasing hnRNP U protein abundance**."
hnRNP U binds HIV-1 mRNA and suppresses its translation to support latency; FBXO34-driven ubiquitination/degradation of hnRNP U abolishes this interaction and relieves the translational block.

"Mechanistically, the authors report that hnRNP U binds HIV-1 mRNA (Rev element region; amino acids 1–339 of hnRNP U are implicated in the RNA interaction) and **hinders HIV-1 translation**, supporting latency; FBXO34-driven ubiquitination/degradation of hnRNP U abolishes this interaction and thus relieves the translational block."
In mouse oocytes Fbxo34 regulates meiotic cell-cycle progression upstream of CCNB1/MPF; depletion lowers MPF activity (rescued by CCNB1) while overexpression triggers spindle-assembly-checkpoint activation and metaphase-I arrest, but no direct substrate was identified.

"In mouse oocytes, Fbxo34 perturbation suggests an important role in meiotic cell-cycle progression: depletion causes failure of meiotic resumption associated with low maturation-promoting factor (MPF) activity and can be rescued by exogenous CCNB1; overexpression promotes GVBD but causes SAC activation and MI arrest."
In mouse oocytes FBXO34 was reported to localize mainly in the nucleus and to colocalize with F-actin during meiotic maturation, providing an orthology-based localization hypothesis for human FBXO34.

"In mouse oocytes, FBXO34 was reported to localize mainly in the **nucleus** and to **colocalize with F-actin** during meiotic maturation."