NDLI: The Carboxyl-terminal Tail of Noxa Protein Regulates the Stability of Noxa and Mcl-1

Content Provider	Journal of Biological Chemistry (JBC)
Author	Pang, Xiaming Zhang, Jingjing Lopez, Hernando Wang, Yushu Li, Wenyang O'Neill, Katelyn L. Evans, Jacquelynn J. D. George, Nicholas M. Long, Jianhong Chen, Yi Luo, Xu
Abstract	The BH3-only protein Noxa is a critical mediator of apoptosis and functions primarily by sequestering/inactivating the antiapoptotic Bcl-2 family protein Mcl-1. Although Noxa is a highly labile protein, recent studies suggested that it is degraded by the proteasome in a ubiquitylation-independent manner. In the present study, we investigated the mechanism of Noxa degradation and its ability to regulate the stability of Mcl-1. We found that the ubiquitylation-independent degradation of Noxa does not require a physical association with Mcl-1. A short stretch of amino acid residues in the C-terminal tail was found to mediate the proteasome-dependent degradation of Noxa. Ectopic placement of this degron was able to render other proteins unstable. Surprisingly, mutation of this sequence not only attenuated the rapid degradation of Noxa, but also stabilized endogenous Mcl-1 through the BH3-mediated direct interaction. Together, these results suggest that the C-terminal tail of Noxa regulates the stability of both Noxa and Mcl-1.
Related Links	http://www.jbc.org/content/289/25/17802.abstract
Ending Page	17811
Starting Page	17802
Page Count	10
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	25
Volume Number	289
DOI	10.1074/jbc.M114.548172
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2014-06-20
Access Restriction	Open
Subject Keyword	Bcl-2 Family Proteins Mitochondrial Apoptosis Protein Complex Protein Stability Ubiquitylation (Ubiquitination) BH3-only Proteins Mcl-1 Noxa Protein Synthesis and Degradation
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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p14ARF-induced Apoptosis in p53 Protein-deficient Cells Is Mediated by BH3-only Protein-independent Derepression of Bak Protein through Down-regulation of Mcl-1 and Bcl-xL Proteins

The carboxyl-terminal tail of Noxa protein regulates the stability of Noxa and Mcl-1.

The Carboxyl-terminal Tail of Noxa Protein Regulates the Stability of Noxa and Mcl-1*

A novel BH3 ligand that selectively targets Mcl-1 reveals that apoptosis can proceed without Mcl-1 degradation

Mouse Noxa uses only the C-terminal BH3-domain to inactivate Mcl-1

ORIGINAL PAPER Apoptosis induced by overall metabolic stress converges on the Bcl-2 family proteins Noxa and Mcl-1 (2011)

The C-terminal Domains of Apoptotic BH3-only Proteins Mediate Their Insertion into Distinct Biological Membranes

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Perturbation of the Bcl-2 Network and an Induced Noxa/Bcl-xL Interaction Trigger Mitochondrial Dysfunction after DNA Damage

The Carboxyl-terminal Tail of Noxa Protein Regulates the Stability of Noxa and Mcl-1

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