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Cell-Surface MuSK Self-Association:a Crucial Role for the Putative Signal Sequence

机译：细胞表面MuSK自缔合：假定信号序列的关键作用。

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The receptor tyrosine kinase MuSK plays a crucial role-both as a signaling molecule and structurally-in the process of clustering nicotinic acetylcholine receptors at the neuromuscular junction.Immunofluorescence microscopy of transiently transfected fibroblasts has been used to visualize the cell-surface distribution of MuSK,which is found in discrete,punctate clusters.This distribution does not result from targeting of MuSK to identified plasma membrane subdomains,and MuSK's association with itself is specific,as MuSK clusters at the cell surface are segregated from clusters of other cotransfected receptor tyrosine kinases.A mutational analysis,using coexpressed pairs of MuSK mutants and chimeras,demonstrates that the putative signal peptide is both necessary and sufficient for association with MuSK.Removal of the intracellular domain or most of the extracellular domain,or replacement of the transmembrane domain,does not abolish MuSK self-association.The N-terminus of the MuSK protein,however,is sufficient to recruit another receptor tyrosine kinase to MuSK clusters.Quantitation and statistical analysis of the amount of colocalization between coexpressed MuSK mutants and chimeras confirm these results.

机译：酪氨酸激酶MuSK在神经肌肉接头聚集烟碱乙酰胆碱受体的过程中起着至关重要的作用-既是信号传导分子，又在结构上起着至关重要的作用。瞬时转染的成纤维细胞的免疫荧光显微镜术已用于观察MuSK的细胞表面分布，这种分布不是由于MuSK靶向已识别的质膜亚结构域而引起的，并且MuSK与自身的缔合是特定的，因为细胞表面的MuSK簇与其他共转染的受体酪氨酸激酶簇分开。使用共表达的MuSK突变体和嵌合体对进行突变分析，表明推定的信号肽对于与MuSK缔合是必要且充分的。细胞内结构域或大部分细胞外结构域的去除或跨膜结构域的取代并没有废除MuSK自缔合.MuSK蛋白的N末端然而，n足以将另一个受体酪氨酸激酶募集到MuSK簇中。共表达的MuSK突变体和嵌合体之间的共定位量的定量和统计分析证实了这些结果。

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《Biochemistry》 |2005年第49期|共10页
作者
Michael J.Bianchetta; Rebecca A.Betensky; Jonathan B.Cohen;
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1. Cell-Surface MuSK Self-Association:a Crucial Role for the Putative Signal Sequence [J] . Michael J.Bianchetta, Rebecca A.Betensky, Jonathan B.Cohen Biochemistry . 2005,第49期

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