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

Nedd4, a human ubiquitin ligase, affects actin cytoskeleton in yeast cells.

Experimental cell research - 1 Nov 2008

Stawiecka-Mirota Marta, Kamińska Joanna, Urban-Grimal Daniele, Haines Dale S, Zoładek Teresa

Abstract excerpt

Human Nedd4 ubiquitin ligase is involved in protein trafficking, signal transduction and oncogenesis. Nedd4 with an inactive WW4 domain is toxic to yeast cells. We report here that actin cytoskeleton is abnormal in yeast cells expressing the NEDD4 or NEDD4w4 gene and these cells are more sensitive to Latrunculin A, an actin-depolymerizing drug. These phenotypes are less pronounced when a mutation inactivating the...

Read the complete abstract on PubMed

Topics

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

Share to Bridged Bicyclo Compounds, Heterocyclic
Share to Cytoskeleton

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endosomal Sorting Complexes Required for Transport

Share to Fluorescent Antibody Technique

Share to Gene Transfer Techniques

Share to Nedd4 Ubiquitin Protein Ligases

Share to Thiazolidines

Share to Wiskott-Aldrich Syndrome Protein

Source

Identifiers

PMID: 18804462
DOI: 10.1016/j.yexcr.2008.08.017

Genes

NEDD4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 10 closest

Nedd4, a human ubiquitin ligase, affects actin cytoskeleton in yeast cells.PMID 18804462Read ↗

The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex.Semantic proximity Read ↗

Substrate proteolysis is inhibited by dominant-negative Nedd4 and Rsp5 mutants harboring alterations in WW domain 1.Semantic proximity Read ↗

Functional analysis of the human orthologue of the RSP5-encoded ubiquitin protein ligase, hNedd4, in yeast.Semantic proximity Read ↗

Saccharomyces cerevisiae Bzz1p Is Implicated with Type I Myosins in Actin Patch Polarization and Is Able To Recruit Actin-Polymerizing Machinery In VitroSemantic proximity Read ↗

Phosphorylation of the WH2 domain in yeast Las17/WASP regulates G-actin binding and protein function during endocytosis.Semantic proximity Read ↗

Mdm20 protein functions with Nat3 protein to acetylate Tpm1 protein and regulate tropomyosin-actin interactions in budding yeast.Semantic proximity Read ↗

Establishment of latrunculin-A resistance in HeLa cells by expression of R183A D184A mutant beta-actin.Semantic proximity Read ↗

New actin mutants allow further characterization of the nucleotide binding cleft and drug binding sites.Semantic proximity Read ↗

WASP suppresses the growth defect of Saccharomyces cerevisiae las17Delta strain in the presence of WIP.Semantic proximity Read ↗

Evidence that proteolysis of Gal4 cannot explain the transcriptional effects of proteasome ATPase mutations.Semantic proximity Read ↗

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