AI Article Synopsis
- The study investigates how CCR5-specific natural antibodies affect the retention of CCR5 receptors in T cells through a mechanism reliant on β-arrestin2 and ERK1, forming a stable CCR5 signalosome for at least 48 hours.
- It highlights that the phosphorylation of CCR5 or ERK1 is crucial for the receptor's internalization into early endosomes, emphasizing the role of the β-arrestin2/ERK1 complex in this signaling process.
- This understanding of CCR5 regulation is important for addressing inflammatory diseases, cancer, and viral infections like HIV.
Article Abstract
The exposure to CCR5 (CC chemokine receptor 5) specific natural antibodies in vitro produces a Class B β-arrestin2-dependent CCR5 retention with the aid of ERK1, due to the formation of a CCR5 signalosome, which remains stable for at least 48 h. Considering that β-arrestins and MAPKs are receptive to environmental signals, their signal complexes could be one of the key junction for GPCRs internalization related signal transduction. Here, we demonstrate that, in T cells, the phosphorylation status of either CCR5 receptor or ERK1 protein is necessary to drive the internalized receptor into the early endosomes, forming the CCR5 signalosome. In particular, our data show that β-arrestin2/ERK1 complex is a relevant transducer in the CCR5 signaling pathway. Understanding the mechanism of CCR5 regulation is essential for many inflammatory disorders, tumorigenesis and viral infection such as HIV.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5795422 | PMC |
| http://dx.doi.org/10.3390/v10010009 | DOI Listing |
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