Unknown

Dataset Information

0

Poly(ADP-ribose)-dependent ubiquitination and its clinical implications.


ABSTRACT: ADP-ribosylation-the addition of one or multiple ADP-ribose units onto proteins-is a therapeutically important post-translational modification implicated in cancer, neurodegeneration, and infectious diseases. The protein modification regulates a broad range of biological processes, including DNA repair, transcription, RNA metabolism, and the structural integrity of nonmembranous structures. The polymeric form of ADP-ribose, poly(ADP-ribose), was recently identified as a signal for triggering protein degradation through the ubiquitin-proteasome system. Using informatics analyses, we found that these ubiquitinated substrates tend to be low abundance proteins, which may serve as rate-limiting factors within signaling networks or metabolic processes. In this review, we summarize the current literature on poly(ADP-ribose)-dependent ubiquitination (PARdU) regarding its biological mechanisms, substrates, and relevance to diseases.

SUBMITTER: Vivelo CA 

PROVIDER: S-EPMC6702056 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Poly(ADP-ribose)-dependent ubiquitination and its clinical implications.

Vivelo Christina A CA   Ayyappan Vinay V   Leung Anthony K L AKL  

Biochemical pharmacology 20190508


ADP-ribosylation-the addition of one or multiple ADP-ribose units onto proteins-is a therapeutically important post-translational modification implicated in cancer, neurodegeneration, and infectious diseases. The protein modification regulates a broad range of biological processes, including DNA repair, transcription, RNA metabolism, and the structural integrity of nonmembranous structures. The polymeric form of ADP-ribose, poly(ADP-ribose), was recently identified as a signal for triggering pro  ...[more]

Similar Datasets

| S-EPMC3278890 | biostudies-literature
| S-EPMC2719406 | biostudies-literature
| S-EPMC2602769 | biostudies-literature
| S-EPMC4794993 | biostudies-literature
| S-EPMC2881810 | biostudies-literature
| S-EPMC6089346 | biostudies-literature
| S-EPMC3351285 | biostudies-literature
| S-EPMC6484711 | biostudies-literature
| S-EPMC3319983 | biostudies-literature
| S-EPMC1563857 | biostudies-literature