Author Correction: Structural dynamics of the midnolin-proteasome during ubiquitin-independent substrate turnover

Following publication, some text has been updated for clarity. In the abstract, “Our structures reveal that midnolin binds to the proteasome via the RPN1 subunit by its C-terminal helix, and its ubiquitin-like domain interacts with the RPN11 deubiquitinase in a non-catalytic role” now replaces the original “Our structures reveal that midnolin binds to the proteasome via the RPN1 subunit by its C-terminal helix. Unexpectedly, its ubiquitin-like domain interacts with the RPN11 deubiquitinase in a non-catalytic role.” In the second paragraph, “The Ubl domain of midnolin is essential for degradation activity. However, unlike canonical shuttle factors such as Rad23 and ubiquilins, which use their Ubl domains to bind the proteasome, the midnolin Ubl domain is dispensable for proteasome and substrate binding” now replaces “Paradoxically, the Ubl domain, which is essential for degradation activity, is dispensable for substrate and proteasome binding.” In the first paragraph of the “The αHelix-C of midnolin interacts with RPN1 (PSMD2) dynamically” section, “Our cryo-EM analysis is consistent with previous studies 12,13 ,” now replaces the original “Our cryo-EM analysis revealed that different from previous studies, ….” The text is updated in the HTML and PDF versions of the article.