Supplementary Materials

Supplementary Materials for:

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

Sang Mi Shim, Ha Rim Choi, Ki Woon Sung, Yoon Jee Lee, Sung Tae Kim, Daeho Kim, Su Ran Mun, Joonsung Hwang, Hyunjoo Cha-Molstad, Aaron Ciechanover, Bo Yeon Kim,* Yong Tae Kwon*

*Corresponding author. Email: yok5{at}snu.ac.kr (Y.T.K.); bykim{at}kribb.re.kr (B.Y.K.)

This PDF file includes:

  • Fig. S1. A model for the mechanism underlying the turnover and Nt-arginylation of BiP.
  • Fig. S2. The overexpression of ATE1 or knockdown of ATE1 does not induce the UPR.
  • Fig. S3. The knockdown of ERAD components does not induce BiP at the mRNA level.
  • Fig. S4. Validation of knockdown efficiency for ERAD components.
  • Fig. S5. HERP knockdown increases the abundance of R-BiP.
  • Fig. S6. The 54-kDa HERP protein is induced and rapidly degraded under ER stress.
  • Table S1. Sequences of the primers used in this study.

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Citation: S. M. Shim, H. R. Choi, K. W. Sung, Y. J. Lee, S. T. Kim, D. Kim, S. R. Mun, J. Hwang, H. Cha-Molstad, A. Ciechanover, B. Y. Kim, Y. T. Kwon, The endoplasmic reticulum–residing chaperone BiP is short-lived and metabolized through N-terminal arginylation. Sci. Signal. 11, eaan0630 (2018).

© 2018 American Association for the Advancement of Science