AI Article Synopsis
- Protein tyrosine phosphatase 1B (PTP1B) is known to negatively regulate leptin and insulin signaling, and mice without PTP1B are resistant to obesity and diabetes.
- Recent findings suggest PTP1B has a new function related to its presence on the endoplasmic reticulum membrane, rather than just its phosphatase activity.
- PTP1B-deficient immune cells produced lower amounts of type I interferon (IFN) when activated, indicating that PTP1B plays a role in enhancing the secretion of antiviral cytokines.
Article Abstract
Protein tyrosine phosphatase 1B (PTP1B, also known as PTPN1) is a negative regulator of the leptin and insulin signalling pathways. This phosphatase is of great interest as PTP1B-knockout mice are protected against the development of obesity and diabetes. Here, we provide evidence for a novel function of PTP1B that is independent of its phosphatase activity, but requires its localisation to the membrane of the endoplasmic reticulum. Upon activation of pattern recognition receptors, macrophages and plasmacytoid dendritic cells from PTP1B-knockout mice secrete lower amounts of type I interferon (IFN) than cells from wild-type mice. In contrast, secretion of the proinflammatory cytokines TNFα and IL6 was unaltered. While PTP1B deficiency did not affect transcription, type I IFN accumulated in macrophages, suggesting a role for PTP1B in mediating secretion of type I IFN. In summary, we have uncovered that PTP1B positively regulates the type I IFN response by promoting secretion of key antiviral cytokines.
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| http://dx.doi.org/10.1242/jcs.246421 | DOI Listing |
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