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BCL2 — VDAC1

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

Studies that report less than 10 interactions are marked with *

• IRef Dip Interaction: VDAC1 — BCL2 (physical association, anti bait coimmunoprecipitation) Rong et al., Proc Natl Acad Sci U S A 2009*
• Gene Ontology Complexes pore complex: pore complex complex (VDAC2-VDAC1-BAK1-TOMM40L-BCL2) Antonsson et al., Science 1997*, Narita et al., Proc Natl Acad Sci U S A 1998

Text-mined interactions from Literome

Sugiyama et al., Oncogene 2002 (Ion Channel Gating) : We have previously shown that the voltage dependent anion channel ( VDAC ) plays a crucial role in apoptotic changes of the mitochondria and its activity is directly regulated by some Bcl-2 family members, including Bcl-2/Bcl-x ( L ) and Bax/Bak but not Bid
Wei et al., Cell Signal 2009 : In contrast, Bcl-XS ( Ser106Ala ) induces a significant loss of VDAC expression, and cytochrome c- and caspase independent toxicity in the non-neuronal HEK293A cells
Ramanathan et al., Proc Natl Acad Sci U S A 2009 : Bcl-xl, but not VDAC1 , is a kinase substrate for mTOR in vitro, and mTOR regulates the association of Bcl-xl with mTOR