TY - JOUR
T1 - Erratum
T2 - ATG8-Binding UIM Proteins Define a New Class of Autophagy Adaptors and Receptors (Cell (2019) 177(3) (766–781.e24), (S0092867419301588), (10.1016/j.cell.2019.02.009))
AU - Marshall, Richard S.
AU - Hua, Zhihua
AU - Mali, Sujina
AU - McLoughlin, Fionn
AU - Vierstra, Richard D.
N1 - Publisher Copyright:
© 2022 Elsevier Inc.
PY - 2022/3/17
Y1 - 2022/3/17
N2 - (Cell 177, 766–781.e1–e24; April 18, 2019) Our paper reported a new family of autophagy adaptors and receptors that use a ubiquitin-interacting motif (UIM)-related sequence to interact with the autophagic vesicle docking protein ATG8 and described the autophagic degradation of dysfunctional CDC48 complexes that use receptors within this family. We subsequently became aware of errors in Figures 7 and S1. During the preparation of Figure 7D (top), we inadvertently duplicated the anti-histone H3 immunoblot provided as a loading control from Figure 7A, rather than showing the correct blot for this experiment. A revised version of Figure 7D (top) containing the correct anti-histone H3 immunoblot is included below. Also, during the preparation of Figure S1D, four control bimolecular fluorescence complementation (BiFC) panels were inadvertently duplicated on the bottom row (NYFP-ATG8a (ΔUDS) + CYFP, NYFP + CYFP-ATG8a (ΔUDS), NYFP-ATG3 + CYFP, and NYFP + CYFP-ATG3). While they appear as black images under normal brightness, the duplicated images can be seen by unique patterns of speckles after brightening the images substantially. A revised version of Figure S1D containing the correct BiFC image panels is included below. Both errors did not affect the results in the paper nor the interpretation of the data, and the authors apologize for any confusion these errors may have caused.
AB - (Cell 177, 766–781.e1–e24; April 18, 2019) Our paper reported a new family of autophagy adaptors and receptors that use a ubiquitin-interacting motif (UIM)-related sequence to interact with the autophagic vesicle docking protein ATG8 and described the autophagic degradation of dysfunctional CDC48 complexes that use receptors within this family. We subsequently became aware of errors in Figures 7 and S1. During the preparation of Figure 7D (top), we inadvertently duplicated the anti-histone H3 immunoblot provided as a loading control from Figure 7A, rather than showing the correct blot for this experiment. A revised version of Figure 7D (top) containing the correct anti-histone H3 immunoblot is included below. Also, during the preparation of Figure S1D, four control bimolecular fluorescence complementation (BiFC) panels were inadvertently duplicated on the bottom row (NYFP-ATG8a (ΔUDS) + CYFP, NYFP + CYFP-ATG8a (ΔUDS), NYFP-ATG3 + CYFP, and NYFP + CYFP-ATG3). While they appear as black images under normal brightness, the duplicated images can be seen by unique patterns of speckles after brightening the images substantially. A revised version of Figure S1D containing the correct BiFC image panels is included below. Both errors did not affect the results in the paper nor the interpretation of the data, and the authors apologize for any confusion these errors may have caused.
UR - http://www.scopus.com/inward/record.url?scp=85126336251&partnerID=8YFLogxK
U2 - 10.1016/j.cell.2022.03.002
DO - 10.1016/j.cell.2022.03.002
M3 - Comment/debate
C2 - 35303423
AN - SCOPUS:85126336251
SN - 0092-8674
VL - 185
SP - 1101
EP - 1102
JO - Cell
JF - Cell
IS - 6
ER -