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PIN1 — PML

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

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: PIN1 — PML (physical association, affinity chromatography technology) Reineke et al., Mol Cell Biol 2008*
• IRef Biogrid Interaction: PIN1 — PML (physical association, affinity chromatography technology) Reineke et al., J Biol Chem 2010*
• IRef Biogrid Interaction: PIN1 — PML (direct interaction, pull down) Reineke et al., J Biol Chem 2010*
• IRef Biogrid Interaction: PIN1 — PML (physical association, affinity chromatography technology) Lim et al., J Biol Chem 2011*
• IRef Intact Interaction: PIN1 — PML (physical association, anti tag coimmunoprecipitation) Yuan et al., Cancer Cell 2011
• IRef Intact Interaction: PIN1 — PML (direct interaction, pull down) Yuan et al., Cancer Cell 2011

Text-mined interactions from Literome

Reineke et al., Mol Cell Biol 2008 (Breast Neoplasms...) : Functionally, we show that in the MDA-MB-231 breast cancer cell line modulating levels of Pin1 affects steady-state levels of PML
Lim et al., J Biol Chem 2011 : To further elucidate the mechanisms underlying Pin1 mediated PML degradation, we aimed to identify one or more factors that promote PML phosphorylation ... Here we show that treatment with U0126, an inhibitor of the ERK2 upstream kinases MEK1/2, leads to an increase in PML protein accumulation and an inhibition of the interaction between Pin1 and PML in MDA-MB-231 breast cancer cells ... Using phospho-specific antibodies, we identified Ser-403 and Ser-505 as the ERK2 targets that promote Pin1 mediated PML degradation ... Taken together, our results support a model in which Pin1 promotes PML degradation in an ERK2 dependent manner