BAIT

PML

MYL, PP8675, RNF71, TRIM19
promyelocytic leukemia
GO Process (39)
GO Function (8)
GO Component (9)

Gene Ontology Biological Process

Homo sapiens

Co-localization

Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.

Publication

A Cellular System that Degrades Misfolded Proteins and Protects against Neurodegeneration.

Guo L, Giasson BI, Glavis-Bloom A, Brewer MD, Shorter J, Gitler AD, Yang X

Misfolded proteins compromise cellular function and cause disease. How these proteins are detected and degraded is not well understood. Here we show that PML/TRIM19 and the SUMO-dependent ubiquitin ligase RNF4 act together to promote the degradation of misfolded proteins in the mammalian cell nucleus. PML selectively interacts with misfolded proteins through distinct substrate recognition sites and conjugates these proteins with ... [more]

Mol. Cell May. 28, 2014; 0(0); [Pubmed: 24882209]

Throughput

  • Low Throughput

Additional Notes

  • All five PML isoforms colocalized with Atxn1 82Q variant aggregates in vivo

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
PML ATXN1
Biochemical Activity
Biochemical Activity

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Low-BioGRID
947969

Curated By

  • BioGRID