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. 2014 Aug 18;206(4):559–572. doi: 10.1083/jcb.201401094

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© 2014 Fernandes and Schöck

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 4. — Localization of mutant Lasp proteins in Lasp¹ mutant background in IFM and BWM. (A) Schematic representation of all Lasp proteins. Orange box, Flag/His tag; blue box, LIM domain; pink boxes, nebulin repeats; green box, SH3 domain. Localization of mutant Lasp proteins is shown in a Lasp¹ mutant background in IFM myofibrils (B) or larval BWM (C). Z-discs are visualized by anti-Kettin antibody staining (blue), Lasp proteins with anti-Flag antibody staining (green), and thin filaments with phalloidin (magenta) in the merged image. (B) In IFM, all Lasp proteins localize to the Z-disc (open arrowheads). Deletion of the LIM domain (L.LaspΔLIM) slightly impairs localization, which appears more diffuse across the thin filaments. (C) In BWM, all Lasp proteins localize to the Z-disc (open arrowheads). The LIM domain deletion (L.LaspΔLIM) and the point mutation in the first nebulin repeat (L.Lasp^Y86S) also localize to the A-band (bracket). The nebulin domain deletion (L.LaspΔNEB12), the SH3 domain deletion (L.LaspΔSH3), and the point mutation in the second nebulin repeat (L.Lasp^Y121S) disrupt A-band localization. Moreover, the deletion of the SH3 domain leads to a weaker Z-disc localization of Lasp. Closed arrowheads indicate the M-line. Bars, 5 µm. Data shown are from larvae or 3-d-old adults.