Cdc48-Ufd1-Npl4: stuck in the middle with Ub.

Bays NW; Hampton RY

doi:10.1016/s0960-9822(02)00862-x

Abstract

The ubiquitin-proteasome pathway has a well-defined beginning and end. Target proteins are initially recognized by upstream components and tagged with polyubiquitin chains. The 26S proteasome then degrades these polyubiquitinated proteins. Until recently, it was not known what, if any, steps occurred between the initial polyubiquitination of target proteins and their final degradation. Several new papers investigating the function of the Cdc48-Ufd1-Npl4 complex indicate that there is indeed a middle to the ubiquitin-proteasome pathway. The Cdc48-Ufd1-Npl4 complex functions in the recognition of several polyubiquitin-tagged proteins and facilitates their presentation to the 26S proteasome for processive degradation or even more specific processing. The elucidation of Cdc48, Ufd1 and Npl4 action not only provides long-sought functions for these specific proteins, but illuminates a poorly understood part of the ubiquitin-proteasome pathway.

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Proteins in UniProt (3)

Cell division control protein 48(UniProt - P25694)
Nuclear protein localization protein 4(UniProt - P33755)
Ubiquitin fusion degradation protein 1(UniProt - P53044)

Saccharomyces Genome Database

https://www.yeastgenome.org/reference/S000071485

Search life-sciences literature (45,103,589 articles, preprints and more)

Cdc48-Ufd1-Npl4: stuck in the middle with Ub.

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Authors

Abstract

Full text links

References

Pathways of ubiquitin conjugation.

The proteasome: a macromolecular assembly designed for controlled proteolysis.

Themes and variations on ubiquitylation.

The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover.

Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1.

Purification and characterization of the 26S proteasome complex catalyzing ATP-dependent breakdown of ubiquitin-ligated proteins from rat liver

Nuclear transport defects and nuclear envelope alterations are associated with mutation of the Saccharomyces cerevisiae NPL4 gene.

A temperature-sensitive NUP116 null mutant forms a nuclear envelope seal over the yeast nuclear pore complex thereby blocking nucleocytoplasmic traffic.

The yeast nuclear pore complex: composition, architecture, and transport mechanism.

Genetic analysis of macromolecular transport across the nuclear envelope.

Citations & impact

Impact metrics

Citations of article over time

Article citations

Genetic Screening of Targeted Region on the Chromosome 22q11.2 in Patients with Microtia and Congenital Heart Defect.

SUMO enhances unfolding of SUMO-polyubiquitin-modified substrates by the Ufd1/Npl4/Cdc48 complex.

An expanded lexicon for the ubiquitin code.

RNA Sequencing Reveals Widespread Transcription of Natural Antisense RNAs in Entamoeba Species.

A Retrotranslocation Assay That Predicts Defective VCP/p97-Mediated Trafficking of a Retroviral Signal Peptide.

Data

Data that cites the article

Proteins in UniProt (3)

Saccharomyces Genome Database

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Search life-sciences literature (45,103,589 articles, preprints and more)

Cdc48-Ufd1-Npl4: stuck in the middle with Ub.

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Abstract

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References

Purification and characterization of the 26S proteasome complex catalyzing ATP-dependent breakdown of ubiquitin-ligated proteins from rat liver

Citations & impact

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Citations of article over time

Article citations

Data

Data that cites the article

Proteins in UniProt (3)

Saccharomyces Genome Database

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