NDLI: Loss of TRB3 alters dynamics of MLK3-JNK signaling and inhibits cytokine-activated pancreatic beta cell death.

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Loss of TRB3 alters dynamics of MLK3-JNK signaling and inhibits cytokine-activated pancreatic beta cell death.

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Loss of TRB3 alters dynamics of MLK3-JNK signaling and inhibits cytokine-activated pancreatic beta cell death.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Jhala, Ulupi S. Ray, Anamika Hao, Ergeng Humphrey, Rohan K. Gonuguntla, Sumati
Description	Author Affiliation: Humphrey RK ( From the Pediatric Diabetes Research Center, University of California, San Diego School of Medicine, La Jolla, California 92037.); Ray A ( From the Pediatric Diabetes Research Center, University of California, San Diego School of Medicine, La Jolla, California 92037.); Gonuguntla S ( From the Pediatric Diabetes Research Center, University of California, San Diego School of Medicine, La Jolla, California 92037.); Hao E ( From the Pediatric Diabetes Research Center, University of California, San Diego School of Medicine, La Jolla, California 92037.); Jhala US ( From the Pediatric Diabetes Research Center, University of California, San Diego School of Medicine, La Jolla, California 92037 ujhala@ucsd.edu.)
Abstract	Disabling cellular defense mechanisms is essential for induction of apoptosis. We have previously shown that cytokine-mediated activation of the MAP3K MLK3 stabilizes TRB3 protein levels to inhibit AKT and compromise beta cell survival. Here, we show that genetic deletion of TRB3 results in basal activation of AKT, preserves mitochondrial integrity, and confers resistance against cytokine-induced pancreatic beta cell death. Mechanistically, we find that TRB3 stabilizes MLK3, most likely by suppressing AKT-directed phosphorylation, ubiquitination, and proteasomal degradation of MLK3. Accordingly, TRB3(-/-) islets show a decrease in both the amplitude and duration of cytokine-stimulated MLK3 induction and JNK activation. It is well known that JNK signaling is facilitated by a feed forward loop of sequential kinase phosphorylation and is reinforced by a mutual stabilization of the module components. The failure of TRB3(-/-) islets to mount an optimal JNK activation response, coupled with the ability of TRB3 to engage and maintain steady state levels of MLK3, recasts TRB3 as an integral functional component of the JNK module in pancreatic beta cells.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	43
Volume Number	289
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2014-10-24
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cell Cycle Proteins Deficiency Cytokines Pharmacology Insulin-Secreting Cells Enzymology Pathology JNK Mitogen-Activated Protein Kinases Metabolism MAP Kinase Kinase Kinases MAP Kinase Signaling System Drug Effects Animals Cell Death Cell Line, Tumor Enzyme Activation Enzyme Stability Insulin Lysine Mice Mutation Genetics Phosphorylation Phosphothreonine Polyubiquitin Proto-Oncogene Proteins C-akt Ubiquitination Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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