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The CHORD protein CHP-1 regulates EGF receptor trafficking and signaling in and human cells.

07:00 EST 13th February 2020 | BioPortfolio

Summary of "The CHORD protein CHP-1 regulates EGF receptor trafficking and signaling in and human cells."

The intracellular trafficking of growth factor receptors determines the activity of their downstream signaling pathways. Here, we show that he putative HSP-90 co-chaperone CHP-1 acts as a regulator of EGFR trafficking in . Loss of causes the retention of the EGFR in the ER and decreases MAPK signaling. CHP-1 is specifically required for EGFR trafficking, as the localization of other transmembrane receptors is unaltered in mutants, and the inhibition of or other co-chaperones does not affect EGFR localization. The role of the CHP-1 homolog CHORDC1 during EGFR trafficking is conserved in human cells. Analogous to , the response of CHORDC1-deficient A431 cells to EGF stimulation is attenuated, the EGFR accumulates in the ER and ERK2 activity decreases. Although CHP-1 has been proposed to act as a co-chaperone for HSP90, our data indicate that CHP-1 plays an HSP90-independent function in controlling EGFR trafficking through the ER.

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This article was published in the following journal.

Name: eLife
ISSN: 2050-084X
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