Cell Signaling and Stress Responses

被引:353
作者
Hotamisligil, Gokhan S. [1 ]
Davis, Roger J. [2 ,3 ]
机构
[1] Harvard Sch Publ Hlth, Broad Inst Harvard MIT, Dept Genet & Complex Dis, Boston, MA 02115 USA
[2] Univ Massachusetts, Sch Med, Howard Hughes Med Inst, Worcester, MA 01605 USA
[3] Univ Massachusetts, Sch Med, Program Mol Med, Worcester, MA 01605 USA
基金
美国国家卫生研究院;
关键词
ENDOPLASMIC-RETICULUM STRESS; UNFOLDED PROTEIN RESPONSE; NF-KAPPA-B; THIOREDOXIN-INTERACTING PROTEIN; NH2-TERMINAL KINASE (JNK)1; INDUCED INSULIN-RESISTANCE; JIP1 SCAFFOLD PROTEIN; BOX-BINDING PROTEIN-1; ER STRESS; MAP-KINASE;
D O I
10.1101/cshperspect.a006072
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Stress-signaling pathways are evolutionarily conserved and play an important role in the maintenance of homeostasis. These pathways are also critical for adaptation to new cellular environments. The endoplasmic reticulum (ER) unfolded protein response (UPR) is activated by biosynthetic stress and leads to a compensatory increase in ER function. The JNK and p38 MAPK signaling pathways control adaptive responses to intracellular and extracellular stresses, including environmental changes such as UV light, heat, and hyperosmotic conditions, and exposure to inflammatory cytokines. Metabolic stress caused by a high-fat diet represents an example of a stimulus that coordinately activates both the UPR and JNK/p38 signaling pathways. Chronic activation of these stress-response pathways ultimately causes metabolic changes associated with obesity and altered insulin sensitivity. Stress-signaling pathways, therefore, represent potential targets for therapeutic intervention in the metabolic stress response and other disease processes.
引用
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页数:20
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