Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2018 May 11;42(2):905–918. doi: 10.3892/ijmm.2018.3672

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright: © Chu et al.

This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

PMC Copyright notice

Proposed mechanism of Ser156 phosphorylation as an allosteric site to modulate a BH3-like domain on BCL2L12 in glioma cells. When BCL2/BCL-XL interacts with the Beclin-1 BH3 domain, autophagy is inhibited. Overexpression of BCL2L12 may displace Beclin-1 in integrating with BCL2/BCL-XL via its BH3-like domain, leading to release of Beclin-1 and initiation of the autophagy process. In addition, since BCL2L12 occupies the hydrophobic groove of BCL2/BCL-XL, BH3 only BCL2 activator or sensitizer is unable to gain access, and the gross result of anti-apoptosis is observed. The BH3 domain mimetic agent, ABT-737, also binds to BCL2/BCL-XL, and hence competes and disrupts the interaction between BCL2/BCL-XL and BCL2L12, making tumor cells more vulnerable to apoptosis. Of note, GSK3β-mediated BCL2L12 S156 phosphorylation may affect BH3 domain function in glioma cells. BCL2L12, BCL2-like 12; BCL2, BCL2 apoptosis regulator; BCL-XL, BCL-extra large; GSK3β, glycogen synthase kinase 3β.