Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Doa1 is a Cdc48 adapter that possesses a novel ubiquitin binding domain.

Molecular and cellular biology - 1 Feb 2006

Mullally James E, Chernova Tatiana, Wilkinson Keith D

Abstract excerpt

Cdc48 (p97/VCP) is an AAA-ATPase molecular chaperone whose cellular functions are facilitated by its interaction with ubiquitin binding cofactors (e.g., Npl4-Ufd1 and Shp1). Several studies have shown that Saccharomyces cerevisiae Doa1 (Ufd3/Zzz4) and its mammalian homologue, PLAA, interact with Cdc48. However, the function of this interaction has not been determined, nor has a physiological link between these...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adaptor Proteins, Signal Transducing
Share to Adenosine Triphosphatases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cell Cycle Proteins

Share to Genetic Complementation Test

Share to Protein Interaction Mapping

Share to Saccharomyces cerevisiae Proteins

Share to Ubiquitin

Share to Valosin Containing Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 16428438
DOI: 10.1128/MCB.26.3.822-830.2006
PMCID: PMC1347030

Genes

PLAA
VCP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Doa1 is a Cdc48 adapter that possesses a novel ubiquitin binding domain.PMID 16428438Read ↗

Structure and function of the PLAA/Ufd3-p97/Cdc48 complex.Semantic proximity Read ↗

The AAA ATPase p97/VCP interacts with its alternative co-factors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism.Semantic proximity Read ↗

Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites.Semantic proximity Read ↗

Cdc48: A Swiss Army Knife of Cell BiologySemantic proximity Read ↗

An Armadillo motif in Ufd3 interacts with Cdc48 and is involved in ubiquitin homeostasis and protein degradation.Semantic proximity Read ↗

DOA1/UFD3 plays a role in sorting ubiquitinated membrane proteins into multivesicular bodies.Semantic proximity Read ↗

The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene.Semantic proximity Read ↗

Cellular functions of Ufd2 and Ufd3 in proteasomal protein degradation depend on Cdc48 binding.Semantic proximity Read ↗

The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast.Semantic proximity Read ↗

The ubiquitin-selective chaperone Cdc48/p97 associates with Ubx3 to modulate monoubiquitylation of histone H2B.Semantic proximity Read ↗

A complex of mammalian Ufd1 and Npl4 links the AAA‐ATPase, p97, to ubiquitin and nuclear transport pathwaysSemantic proximity Read ↗

Control of p97 function by cofactor binding.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.