Unknown

Dataset Information

0

The PML nuclear bodies-associated protein TTRAP regulates ribosome biogenesis in nucleolar cavities upon proteasome inhibition.


ABSTRACT: TRAF and TNF receptor-associated protein (TTRAP) is a multifunctional protein that can act in the nucleus as a 5'-tyrosyl DNA phosphodiesterase and in the cytoplasm as a regulator of cell signaling. In this paper we show that in response to proteasome inhibition TTRAP accumulates in nucleolar cavities in a promyelocytic leukemia protein-dependent manner. In the nucleolus, TTRAP contributes to control levels of ribosomal RNA precursor and processing intermediates, and this phenotype is independent from its 5'-tyrosyl DNA phosphodiesterase activity. Our findings suggest a previously unidentified function for TTRAP and nucleolar cavities in ribosome biogenesis under stress.

SUBMITTER: Vilotti S 

PROVIDER: S-EPMC3278732 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

The PML nuclear bodies-associated protein TTRAP regulates ribosome biogenesis in nucleolar cavities upon proteasome inhibition.

Vilotti S S   Biagioli M M   Foti R R   Dal Ferro M M   Lavina Z Scotto ZS   Collavin L L   Del Sal G G   Zucchelli S S   Gustincich S S  

Cell death and differentiation 20110916 3


TRAF and TNF receptor-associated protein (TTRAP) is a multifunctional protein that can act in the nucleus as a 5'-tyrosyl DNA phosphodiesterase and in the cytoplasm as a regulator of cell signaling. In this paper we show that in response to proteasome inhibition TTRAP accumulates in nucleolar cavities in a promyelocytic leukemia protein-dependent manner. In the nucleolus, TTRAP contributes to control levels of ribosomal RNA precursor and processing intermediates, and this phenotype is independen  ...[more]

Similar Datasets

| S-EPMC4615814 | biostudies-literature
| S-EPMC5691659 | biostudies-literature
| S-EPMC10575996 | biostudies-literature
| S-EPMC4615761 | biostudies-literature
| S-EPMC7486236 | biostudies-literature
| S-EPMC6706441 | biostudies-literature
| S-EPMC4876461 | biostudies-literature
| S-EPMC7601244 | biostudies-literature
| S-EPMC3984170 | biostudies-literature
| S-EPMC2993750 | biostudies-literature