Blockade of the BAK hydrophobic groove by inhibitory phosphorylation regulates commitment to apoptosis
The BCL-2 family protein BAK is a key regulator of mitochondrial apoptosis. BAK activation first involves N-terminal conformational changes that lead to the transient exposure of the BAK BH3 domain that then inserts into a hydrophobic groove on another BAK molecule to form symmetric dimers. We showe...
Main Authors: | Azad, A, Fox, J, Leverrier, S, Storey, A |
---|---|
Format: | Journal article |
Language: | English |
Published: |
Public Library of Science
2012
|
Similar Items
-
Tyrosine dephosphorylation is required for Bak activation in apoptosis.
by: Fox, J, et al.
Published: (2010) -
Tyrosine dephosphorylation is required for Bak activation in apoptosis
by: Fox, J, et al.
Published: (2010) -
"Licensed to kill": tyrosine dephosphorylation and Bak activation.
by: Fox, J, et al.
Published: (2011) -
Parkin-mediated ubiquitination inhibits BAK apoptotic activity by blocking its canonical hydrophobic groove
by: Peng Cheng, et al.
Published: (2023-12-01) -
Identification of the regions of the HPV 5 E6 protein involved in Bak degradation and inhibition of apoptosis.
by: Simmonds, M, et al.
Published: (2008)