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Journal of Cell Science logoLink to Journal of Cell Science
. 2019 Mar 28;132(6):jcs231746. doi: 10.1242/jcs.231746

Correction: The PIKfyve complex regulates the early melanosome homeostasis required for physiological amyloid formation (doi:10.1242/jcs.229500)

Christin Bissig, Pauline Croisé, Xavier Heiligenstein, Ilse Hurbain, Guy M Lenk, Emily Kaufman, Ragna Sannerud, Wim Annaert, Miriam H Meisler, Lois S Weisman, Graça Raposo, Guillaume van Niel
PMCID: PMC6919642  PMID: 30923131

There was an error in J. Cell Sci. (2019) 132, jcs229500 (doi:10.1242/jcs.229500).

The DMSO lanes in Fig. 2C and D were duplicated in Fig. 2E and F, respectively, which contravenes our image presentation guidelines. The authors supplied full blots for all these panels and prepared a new figure using these.

Fig. 2 (original panels).

Fig. 2 (original panels).

M-α fragments accumulate upon interference with PIKfyve function or lysosomal protease activity. (C–F) MNT-1 cells were treated for 2 h or 24 h with 1.6 µM YM201636 (C,D) or with a mixture of protease inhibitors (100 µM leupeptin, 10 µM pepstatin A and 10 µM E-64d) (E,F) and Triton X-100-soluble (C,E) and Triton X-100-insoluble (D,F) lysates were analyzed by immunoblotting using antibodies against the PMEL C-terminus (anti-PMEL-C), the PMEL N-terminus (anti-PMEL-N), the PMEL RPT domain (anti-PMEL-HMB45), the PMEL PKD domain (anti-PMEL-I51) and tubulin (anti-TUB), as an equal loading marker. The different PMEL fragments are annotated on the right. Stars indicate M-α fragments derived from another isoform generated by alternative splicing. Right-hand panels show higher exposures.

The corrected and original panels are shown below. Both the online full-text and PDF versions of the article have been updated.

Fig. 2 (corrected panels).

Fig. 2 (corrected panels).

M-α fragments accumulate upon interference with PIKfyve function or lysosomal protease activity. (C,D) MNT-1 cells were treated for 2 h or 24 h with 1.6 µM YM201636 or with a mixture of protease inhibitors (100 µM leupeptin, 10 µM pepstatin A and 10 µM E-64d) and Triton X-100-soluble (C) and Triton X-100-insoluble (D) lysates were analyzed by immunoblotting using antibodies against the PMEL C-terminus (anti-PMEL-C), the PMEL N-terminus (anti-PMEL-N), the PMEL RPT domain (anti-PMEL-HMB45), the PMEL PKD domain (anti-PMEL-I51) and tubulin (anti-TUB), as an equal loading marker. The different PMEL fragments are annotated on the right. Stars indicate M-α fragments derived from another isoform generated by alternative splicing. Right-hand panels show higher exposures.

The authors apologise for this error.


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