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CORRECTION article

Front. Cell Dev. Biol., 18 August 2023
Sec. Cellular Biochemistry

Corrigendum: Reconstitution of phase-separated signaling clusters and actin polymerization on supported lipid bilayers

  • Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, United States

A Corrigendum on
Reconstitution of phase-separated signaling clusters and actin polymerization on supported lipid bilayers

by Cheng X, Ullo MF and Case LB (2022). Front. Cell Dev. Biol. 10:932483. doi: 10.3389/fcell.2022.932483

In the published article, there was an error in the captions for Figures 4–6 as published. In these captions, “0.25 µM” should be “250 µM.” The corrected captions appears below.

“FIGURE 4 | Actin polymerization from phase separated clusters. (A) Total Internal Reflection Fluorescence (TIRF) imaging of 1 µM actin (5% labeled by Alexa 647, magenta) polymerization with 3 nM Arp2/3, 250 µM ATP, 0.1 mM MgCl2 and 0.1 mM EGTA, from clusters made from 500 nM Nck (15% labeled by Alexa488, green), 250 nM N-WASP and 2.5 nM His8-nephrin on the membrane. (B) Zoom-in view of region indicated by white box in (A). Scale bars, 10 µm. Total Internal Reflection Fluorescence (TIRF) penetration depth 200 nm for all channels.”

“FIGURE 5 | Actin polymerization with different levels of capping proteins. (A) 1 µM actin (5% labeled by Alexa647) polymerization is induced by 3 nM Arp2/3, 250 µM ATP, 0.1 mM MgCl2 and 0.1 mM EGTA, with different amounts of CapZ included in the system (indicated above each image), from clusters made from 500 nM Nck, 250 nM N-WASP and 1.25 nM His8-nephrin (15% labeled by Alexa405) on the membrane. Individual images are TIRF image overlays of nephrin-405 shown in cyan and actin-647 shown in magenta. Total Internal Reflection Fluorescence (TIRF) penetration depth 200 nm for all channels. Scale bar, 5 µm. (B) Quantification of actin mean and fraction intensity over time for the conditions showed in (A). Actin was selected by selecting the intensity threshold between 250 and 65535 the individual 16-bit images, values for each frame are calculated as described in Section 4.4.”

“FIGURE 6 | Representative actin polymerization analysis (A) 1 µM actin (5% labeled by Alexa647) polymerization is induced by 3 nM Arp2/3, 6 nM CapZ, 250 µM ATP, 0.1 mM MgCl2 and 0.1 mM EGTA, from clusters made from 1 µM Nck, 2 μM N-WASP (15% Alexa488) and 1.25 nM His8-nephrin on the membrane. Binary mask from segmentation of the N-WASP images. Pixels outside the clusters are white, pixels inside the clusters are black. Scale bar, 5 µm. (B) Quantification of actin polymerization over time for the condition showed in (A). Graph was generated in Matlab. Black dotted lines indicate a linear fit of the five points around the half-max intensity.”

The authors apologize for these errors and state that this does not change the scientific conclusions of the article in any way. The original article has been updated.

Publisher’s note

All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article, or claim that may be made by its manufacturer, is not guaranteed or endorsed by the publisher.

Keywords: phase separation, supported lipid bilayer, actin, ARP2/3 complex, total internal reflection fluorescence microscopy, biochemical reconstitution

Citation: Cheng X, Ullo MF and Case LB (2023) Corrigendum: Reconstitution of phase-separated signaling clusters and actin polymerization on supported lipid bilayers. Front. Cell Dev. Biol. 11:1274775. doi: 10.3389/fcell.2023.1274775

Received: 08 August 2023; Accepted: 09 August 2023;
Published: 18 August 2023.

Approved by:

Frontiers Editorial Office, Frontiers Media SA, Switzerland

Copyright © 2023 Cheng, Ullo and Case. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

*Correspondence: Lindsay B. Case, lcase@mit.edu

Disclaimer: All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.