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BCL2 — BECN1

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

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: BECN1 — BCL2 (physical association, affinity chromatography technology) Chang et al., EMBO J 2010*
• IRef Biogrid Interaction: BECN1 — BCL2 (physical association, affinity chromatography technology) Chen et al., J Biol Chem 2010*
• IRef Biogrid Interaction: BECN1 — BCL2 (physical association, affinity chromatography technology) Xu et al., FASEB J 2011*
• IRef Biogrid Interaction: BECN1 — BCL2 (physical association, affinity chromatography technology) Strappazzon et al., EMBO J 2011*
• IRef Biogrid Interaction: BECN1 — BCL2 (physical association, affinity chromatography technology) Zhou et al., Acta Pharmacol Sin 2013*
• IRef Biogrid Interaction: BECN1 — BCL2 (physical association, affinity chromatography technology) Molejon et al., Scientific reports 2013*
• IRef Biogrid Interaction: BECN1 — BCL2 (physical association, affinity chromatography technology) Yang et al., Int J Mol Med 2012*
• IRef Biogrid Interaction: BECN1 — BCL2 (physical association, affinity chromatography technology) Trisciuoglio et al., Neoplasia (New York, N.Y.) 2013*
• IRef Biogrid Interaction: BECN1 — BCL2 (physical association, affinity chromatography technology) Han et al., Autophagy 2012*
• IRef Biogrid Interaction: BECN1 — BCL2 (direct interaction, two hybrid) Liang et al., J Virol 1998*
• IRef Biogrid Interaction: BECN1 — BCL2 (direct interaction, fluorescent resonance energy transfer) Liang et al., J Virol 1998*
• IRef Dip Interaction: BECN1 — BCL2 (physical association, anti tag coimmunoprecipitation) Sun et al., Proc Natl Acad Sci U S A 2008
• IRef Dip Interaction: Complex of PIK3C3-BCL2-UVRAG-BECN1 (anti tag coimmunoprecipitation) Sun et al., Proc Natl Acad Sci U S A 2008
• IRef Hprd Interaction: BECN1 — BCL2 (two hybrid) Liang et al., J Virol 1998*
• IRef Hprd Interaction: BECN1 — BCL2 (in vitro) Liang et al., J Virol 1998*
• IRef Hprd Interaction: BECN1 — BCL2 (in vivo) Liang et al., J Virol 1998*
• IRef Innatedb Interaction: BECN1 — BCL2 (unknown, -) Ciechomska et al., Oncogene 2009*
• IRef Innatedb Interaction: BECN1 — BCL2 (unknown, -) Maiuri et al., Autophagy 2007*
• IRef Innatedb Interaction: BECN1 — BCL2 (unknown, -) Sun et al., Proc Natl Acad Sci U S A 2008
• IRef Innatedb Interaction: BECN1 — BCL2 (unknown, -) Pattingre et al., Cell 2005*
• IRef Innatedb Interaction: BECN1 — BCL2 (unknown, -) Bellot et al., Mol Cell Biol 2009*
• IRef Innatedb Interaction: BECN1 — BCL2 (unknown, -) Tang et al., Oncogene 2010*
• IRef Intact Interaction: Complex of DAPK1-BCL2-BECN1 (association, pull down) Zalckvar et al., EMBO Rep 2009*
• IRef Intact Interaction: Complex of BCL2-BECN1-CALR (colocalization, cosedimentation through density gradient) Germain et al., EMBO J 2011*
• IRef Intact Interaction: Complex of CALR-BCL2-HSPA9-MCL1-BECN1 (colocalization, cosedimentation through density gradient) Germain et al., EMBO J 2011*
• IRef Intact Interaction: Complex of BCL2-BECN1-AMBRA1 (association, anti bait coimmunoprecipitation) Strappazzon et al., EMBO J 2011*
• IRef Intact Interaction: Complex of BCL2-BCLAF1-BECN1 (association, anti bait coimmunoprecipitation) Lamy et al., Cancer Cell 2013*
• IRef Intact Interaction: BECN1 — BCL2 (physical association, two hybrid) Maiuri et al., EMBO J 2007*
• IRef Intact Interaction: BECN1 — BCL2 (physical association, anti bait coimmunoprecipitation) Maiuri et al., EMBO J 2007*
• IRef Intact Interaction: BECN1 — BCL2 (physical association, anti bait coimmunoprecipitation) Criollo et al., EMBO J 2010*
• IRef Intact Interaction: BECN1 — BCL2 (physical association, anti tag coimmunoprecipitation) Strappazzon et al., EMBO J 2011*
• IRef Intact Interaction: BECN1 — BCL2 (physical association, anti bait coimmunoprecipitation) Lamy et al., Cancer Cell 2013*
• IRef Intact Interaction: BECN1 — BCL2 (physical association, anti tag coimmunoprecipitation) He et al., Cell 2013
• IRef Ophid Interaction: BECN1 — BCL2 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Liang et al., Nat Cell Biol 2006 (Carcinoma...) : The autophagic activity of the Beclin1-PI(3)KC3 complex, however, is suppressed by Bcl-2 ... UVRAG, a tumour suppressor candidate that is monoallelically mutated at high frequency in human colon cancers, associates with the Beclin1-Bcl-2-PI(3)KC3 multiprotein complex, where UVRAG and Beclin1 interdependently induce autophagy
Hamacher-Brady et al., J Biol Chem 2006 (Myocardial Ischemia...) : Bcl-2 and Bcl-x ( L ) were protective against I/R injury, and expression of a Beclin1 Bcl-2/-x ( L ) binding domain mutant resulted in decreased autophagic flux and did not protect against I/R injury
Brady et al., FEBS J 2007 (Calcium Signaling) : We found that in HL-1 cardiac myocytes the relationship between Beclin 1 and Bcl-2 is subtle : Beclin 1 mutant lacking the Bcl-2 binding domain significantly reduced autophagic activity, indicating that Beclin 1-mediated autophagy required an interaction with Bcl-2
Akar et al., Autophagy 2008 (Breast Neoplasms) : Silencing of Bcl-2 by siRNA also led to induction of LC-3-II, a hallmark of autophagy, ATG5 and Beclin-1 autophagy promoting proteins
Park et al., Biochem Biophys Res Commun 2009 : Here we report that, in the JNK dependent autophagic cell death of HCT116 cells induced by an agonistic single chain variable fragment antibody, HW1, against human death receptor 5 (DR5), JNK activation upregulated Beclin-1 expression and induced Bcl-2 and p53 phosphorylation
Liu et al., J Pharmacol Sci 2012 (Lung Neoplasms) : Moreover, ERK activation upregulated Beclin-1 expression through induction of Bcl-2 phosphorylation, but p53 did not induce Bcl-2 phosphorylation
Robert et al., Autophagy 2012 : It has been previously reported that Bcl-2 and Bcl-X ( L ) bind and inhibit BECN1 , an essential mediator of autophagy
Sun et al., Int J Gynecol Cancer 2012 (Uterine Cervical Neoplasms) : Furthermore, Beclin 1 overexpression resulted in increased cytoplasmic cytochrome c and Bax expression and decreased mitochondrial cytochrome c and Bcl-2 expression
He et al., Diabetes 2013 (Diabetes Mellitus, Experimental...) : Exposure of H9c2 cells to high glucose reduced AMPK activity, inhibited Jun NH2-terminal kinase 1 (JNK1)-B-cell lymphoma 2 (Bcl-2) signaling, and promoted Beclin1 binding to Bcl-2
Zou et al., Biochem J 2013 : Lower levels of Bcl-2 lead to release of more Beclin 1 to form the Beclin 1-PI3KCIII ( class III phosphoinositide 3-kinase ) complex to activate autophagy and accelerate the turnover of dysfunctional mitochondria through the PI3K ( phosphoinositide 3-kinase ) /Akt/mTOR ( mammalian target of rapamycin ) pathway