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

Acetylation of SUMO1 Alters Interactions with the SIMs of PML and Daxx in a Protein-Specific Manner.

Structure (London, England : 1993) - 4 Feb 2020

Mascle Xavier H, Gagnon Christina, Wahba Haytham M, Lussier-Price Mathieu, Cappadocia Laurent, Sakaguchi Kazuyasu, Omichinski James G

Abstract excerpt

The interactions between SUMO proteins and SUMO-interacting motif (SIM) in nuclear bodies formed by the promyelocytic leukemia (PML) protein (PML-NBs) have been shown to be modulated by either phosphorylation of the SIMs or acetylation of SUMO proteins. However, little is known about how this occurs at the atomic level. In this work, we examined the role that acetylation of SUMO1 plays on its binding to the...

Read the complete abstract on PubMed

Topics

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

Share to Acetylation
Share to Co-Repressor Proteins

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

Share to Lysine

Share to Molecular Chaperones

Share to Promyelocytic Leukemia Protein

Share to Protein Domains

Share to Protein Folding

Share to SUMO-1 Protein

Source

Identifiers

PMID: 31879127
DOI: 10.1016/j.str.2019.11.019

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Acetylation of SUMO1 Alters Interactions with the SIMs of PML and Daxx in a Protein-Specific Manner.PMID 31879127Read ↗

Sumoylation in Physiology, Pathology and TherapySemantic proximity Read ↗

The PML-Interacting Protein DAXX: Histone Loading Gets into the PictureSemantic proximity Read ↗

Requirement of PML SUMO interacting motif for RNF4- or arsenic trioxide-induced degradation of nuclear PML isoforms.Semantic proximity Read ↗

The SUMO protease SENP6 is a direct regulator of PML nuclear bodies.Semantic proximity Read ↗

Activation of the SUMO modification system is required for the accumulation of RAD51 at sites containing DNA damageSemantic proximity Read ↗

Effect of SUMO-SIM Interaction on the ICP0-Mediated Degradation of PML Isoform II and Its Associated Proteins in Herpes Simplex Virus 1 Infection.Semantic proximity Read ↗

The protein stability and transcriptional activity of p63alpha are regulated by SUMO-1 conjugation.Semantic proximity Read ↗

Degradation of the tumor suppressor PML by Pin1 contributes to the cancer phenotype of breast cancer MDA-MB-231 cells.Semantic proximity Read ↗

The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA.Semantic proximity Read ↗

Acetylation of PML is involved in histone deacetylase inhibitor-mediated apoptosis.Semantic proximity Read ↗

A small conserved surface in SUMO is the critical structural determinant of its transcriptional inhibitory properties.Semantic proximity Read ↗

Role of the PLDLS-binding cleft region of CtBP1 in recruitment of core and auxiliary components of the corepressor complex.Semantic proximity Read ↗

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