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. 2001 Apr 16;153(2):413–428. doi: 10.1083/jcb.153.2.413

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© 2001 The Rockefeller University Press

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 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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Yeast two-hybrid screens identify myopalladin and desmin as Z-line nebulin-binding proteins. Schematic structure of the COOH-terminal region of nebulin and its location within the sarcomere is shown based on previous immunoelectron microscopy studies (Millevoi et al. 1998). The nebulin COOH-terminal region constructs pAS2-M160-M185+Ser+SH3C and pAS2-M160-M183 identified myopalladin and desmin prey clones in yeast two-hybrid screens. Nebulin bait deletion constructs (NebΔ1–NebΔ3) allowed us to further map the myopalladin-binding region on nebulin to within the nebulin SH3 domain. The desmin-binding site on nebulin was found to be located within the nebulin M160-M183 modules. (+) and (−) denote the presence or absence of the growth of yeast colonies on SD/Trp-/Leu-/His-plates supplemented with 1.5 mM 3-AT.