Abstract
Bcl-G acquitted of murder!
Highlights
Proteins of the Bcl-2 family are characterized by the presence of structural motives, referred to as Bcl-2 homology (BH) domains that orchestrate protein–protein interactions within the family
Sequence analysis of the BH3 domain of Bcl-G in urinary bladder cancer and laryngeal squamous cell carcinomas failed to detect any mutations, suggesting that a possible tumor suppressive role may be unrelated to possible Bcl-2 family interactions,[5,6] and the analysis of the remaining allele of Bcl-G in pre-B childhood acute lymphoblastic leukemia patients that carry a 12p hemizygous deletion failed to reveal any loss-of-function,[7] questioning a role as tumor suppressor
Whereas no significant protein levels were detected in lymphocytes, high expression was observed in CD8 þ conventional dendritic cells (DC), while plasmacytoid DCs lacked Bcl-G
Summary
Proteins of the Bcl-2 family are characterized by the presence of structural motives, referred to as Bcl-2 homology (BH) domains that orchestrate protein–protein interactions within the family. Contrary to Bcl-GS, Bcl-GL possesses a BH2 domain but does not display any significant binding to Bcl-xL, nor apoptotic activity.
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