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PML — RNF4

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: RNF4 — PML (physical association, affinity chromatography technology) Häkli et al., Exp Cell Res 2005*
• IRef Biogrid Interaction: RNF4 — PML (direct interaction, enzymatic study) Tatham et al., Nat Cell Biol 2008*
• IRef Biogrid Interaction: RNF4 — PML (direct interaction, fluorescent resonance energy transfer) Percherancier et al., J Biol Chem 2009*
• IRef Biogrid Interaction: RNF4 — PML (physical association, affinity chromatography technology) Maroui et al., PloS one 2012*
• IRef Biogrid Interaction: RNF4 — PML (direct interaction, fluorescent resonance energy transfer) Maroui et al., PloS one 2012*
• IRef Biogrid Interaction: RNF4 — PML (physical association, affinity chromatography technology) Bruderer et al., EMBO Rep 2011

Text-mined interactions from Literome

Geoffroy et al., Mol Biol Cell 2010 : This initial recruitment of PML into nuclear bodies is not dependent on RNF4, but RNF4 quickly follows PML into the nuclear bodies where it is responsible for ubiquitylation of SUMO modified PML and its degradation by the proteasome
Nagai et al., Cell Res 2011 (Genomic Instability) : The mammalian STUbL RNF4 associates with Promyelocytic leukaemia (PML) nuclear bodies and regulates PML/PML-fusion protein stability in response to arsenic induced stress