Puma*Mcl-1 interaction is not sufficient to prevent rapid degradation of Mcl-1

Endogenous Bak inhibitors Mcl-1 and Bcl-xL: differential impact on TRAIL resistance in Bax-deficient carcinoma

“…In contrast, TRAIL caused increased binding of Bim and Puma to Mcl-1 (Meng et al, 2007). Nevertheless, binding of Bim, Puma, or Nbk has been shown to stabilize Mcl-1 (Mei et al, 2005;Czabotar et al, 2007;Gillissen et al, 2007). Inhibition of proapoptotic Bcl-2 family members by Mcl-1 might therefore be further enforced by increased expression of Mcl-1 induced by TRAIL through activation of the NF-B pathway (Ricci et al, 2007) that would also facilitate expression of Bcl-x L , an NF-B target.…”

NOXA, a sensor of proteasome integrity, is degraded by 26S proteasomes by an ubiquitin-independent pathway that is blocked by MCL-1

“…The basis for these apparently conflicting observations is unclear but may relate to cell type differences, multiplicity of other E3 ligases and deubiquitinases for MCL-1, or MULE may not be present or have access to the NOXA/MCL-1 complex. Two other BH3-only proteins, BIM and PUMA, stabilize MCL-1 via a mechanism that requires their BH3 domains, 21,37 and interaction of BIM EL with BCL-2 also reduces its turnover. 38 Although further studies are required to reconcile these differing results, together they highlight the critical role that interactions between BH3-only proteins and their pro-survival partners have in regulating the stability of multiple BCL-2 family proteins.…”

Optimal dietary protein level improved growth, disease resistance, intestinal immune and physical barrier function of young grass carp (Ctenopharyngodon idella)

“…Slee et al [89] reported that the inhibition of caspase 9 could decrease the expression of caspase 2, caspase 3 and caspase 7 in Jurkat T lymphoblastoid cells. It has been reported that the inhibition of pro-apoptotic Apaf-1 in SF21 insect cells [90] and Bax in HUVECs [91], as well as the increase of anti-apoptotic Bcl-2 in HUVECs [91], Mcl-1 in HeLa cells [92] and IAP in mammalian cells [93], could suppress the activation of caspase 9. Additionally, the inhibition of JNK could decrease pro-apoptotic Bax in kidney cells [94] and increase anti-apoptotic IAP in cancer cells [95] and Mcl-1 in HEK293 cells [96].…”