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000166794 0247_ $$2doi$$a10.1091/mbc.E13-04-0202
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000166794 0247_ $$2ISSN$$a1939-4586
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000166794 1001_ $$0P:(DE-HGF)0$$aEulitz, S.$$b0$$eCorresponding author
000166794 245__ $$aIdentification of Xin-repeat proteins as novel ligands of the SH3 domains of nebulin and nebulette and analysis of their interaction during myofibril formation and remodeling
000166794 260__ $$aBethesda, Md.$$bAmerican Society for Cell Biology$$c2013
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000166794 500__ $$a© Eulitz et al. 
000166794 520__ $$aThe Xin actin-binding repeat-containing proteins Xin and XIRP2 are exclusively expressed in striated muscle cells, where they are believed to play an important role in development. In adult muscle, both proteins are concentrated at attachment sites of myofibrils to the membrane. In contrast, during development they are localized to immature myofibrils together with their binding partner, filamin C, indicating an involvement of both proteins in myofibril assembly. We identify the SH3 domains of nebulin and nebulette as novel ligands of proline-rich regions of Xin and XIRP2. Precise binding motifs are mapped and shown to bind both SH3 domains with micromolar affinity. Cocrystallization of the nebulette SH3 domain with the interacting XIRP2 peptide PPPTLPKPKLPKH reveals selective interactions that conform to class II SH3 domain-binding peptides. Bimolecular fluorescence complementation experiments in cultured muscle cells indicate a temporally restricted interaction of Xin-repeat proteins with nebulin/nebulette during early stages of myofibril development that is lost upon further maturation. In mature myofibrils, this interaction is limited to longitudinally oriented structures associated with myofibril development and remodeling. These data provide new insights into the role of Xin actin-binding repeat-containing proteins (together with their interaction partners) in myofibril assembly and after muscle damage.
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000166794 7001_ $$0P:(DE-H253)PIP1014520$$aSauer, Florian$$b1
000166794 7001_ $$0P:(DE-H253)PIP1014519$$aPelissier, M.-C.$$b2
000166794 7001_ $$0P:(DE-HGF)0$$aBoisguerin, P.$$b3
000166794 7001_ $$0P:(DE-HGF)0$$aMolt, S.$$b4
000166794 7001_ $$0P:(DE-HGF)0$$aSchuld, J.$$b5
000166794 7001_ $$0P:(DE-HGF)0$$aOrfanos, Z.$$b6
000166794 7001_ $$0P:(DE-HGF)0$$aKley, R. A.$$b7
000166794 7001_ $$0P:(DE-HGF)0$$aVolkmer, R.$$b8
000166794 7001_ $$0P:(DE-H253)PIP1001283$$aWilmanns, M.$$b9
000166794 7001_ $$0P:(DE-HGF)0$$aKirfel, G.$$b10
000166794 7001_ $$0P:(DE-HGF)0$$avan der Ven, P. F. M.$$b11
000166794 7001_ $$0P:(DE-HGF)0$$aFurst, D. O.$$b12
000166794 773__ $$0PERI:(DE-600)1474922-1$$a10.1091/mbc.E13-04-0202$$gVol. 24, no. 20, p. 3215 - 3226$$n20$$p3215 - 3226$$tMolecular biology of the cell$$v24$$x1059-1524$$y2013
000166794 8564_ $$uhttps://bib-pubdb1.desy.de/record/166794/files/DESY-2014-01628.pdf$$yPublished on 2013-08-28. Available in OpenAccess from 2013-10-28.
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