Author Correction: The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation

Abstract

The Article mentions but does not include control data demonstrating that a random mutation in the cDNA sequence of DNAJB6b used in the study does not affect the behaviour of its protein product. Specifically, the cDNA sequence of DNAJB6b WT and DNAJB6b H31Q in the plasmids used for all the experiments reported in this study contained a mutation (TTC to TCC) leading to the F46S mutation in the translated proteins, which was randomly introduced during the cloning. The mutation did not change the localisation or ability to inhibit α-syn aggregation in HEK293T-α-syn-dsred cells, as shown in Figure 1 below. This does not affect the conclusions of the Article.

HSP90 Co-Chaperone, CacyBP/SIP, Protects α-Synuclein from Aggregation

“…Chaperones and co-chaperones are essential players in the regulation of cellular proteostasis; in particular, they protect cells from pathogenic aggregation of misfolded proteins [ 34 ]. For instance, it has been shown that, in vitro, HSP70 alone or in cooperation with different chaperones/co-chaperones inhibits formation of α-synuclein fibrils [ 35 , 36 ] and tau aggregates [ 32 ], and reduces polyglutamine (polyQ)-induced toxicity when exogenously added to cultured cells [ 37 ]. Other chaperones such as HSP60 and HSP40 have been shown to suppress α-synuclein fibrillization in vitro and to block the polyQ-induced toxicity, respectively [ 38 , 39 ].…”