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A database built with INDRA combining content from numerous readers and databases. This page allows you to curate the loaded statements. For more information please see the manual.

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INDRA is developed by indralabs, a part of the Harvard Medical School Laboratory of Systems Pharmacology.

This project, indra_db, is also developed by the indralab team. For more information on how we procure our sources, you can go here. This work was funded by ARO grant W911NF‐15‐1‐0544 under the DARPA Communicating with Computers program.

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Endoplasmic reticulum activates USP14. 3 / 3

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"Mechanistically, sustained ER stress up-regulated the deubiquitinating enzyme ubiquitin specific peptidase 14 (USP14), which increased the stability and levels of 3 ',5 '-cyclic monophosphate responsive element binding (CREB) protein (CBP) to enhance glucagon action and hepatic gluconeogenesis."

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"In conclusion, ER stress induces the upregulation of USP14, which leads to the destruction of glucose homeostasis [XREF_BIBR]."

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"Studies have shown that sustained ER stress upregulates USP14 from the transcription level through ATF4, thus improving the stability and level of CREB binding protein CBP, enhancing the role of glucagon and hepatic gluconeogenesis."

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Endoplasmic reticulum activates USP14. 3 / 3

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