Research ArticleStress responses

The endoplasmic reticulum–residing chaperone BiP is short-lived and metabolized through N-terminal arginylation

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Science Signaling  02 Jan 2018:
Vol. 11, Issue 511, eaan0630
DOI: 10.1126/scisignal.aan0630

Instability of the ER-residing proteins

Some ER proteins are subjected to a posttranslational modification known as N-terminal arginylation. Shim et al. found that the ER chaperone BiP was unexpectedly short-lived and that N-terminal arginylation promoted its relocalization to the cytosol, where it was degraded. ER stress, particularly when combined with proteasomal inhibition, increased the N-terminal arginylation of BiP. This pathway was inhibited by HERP, a component of the ER degradation pathway. These results suggest that ER proteins are more unstable than was previously appreciated, which may enable cells to quickly return the abundance of ER chaperones to basal amounts after ER stress has been resolved.

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