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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The receptor protein tyrosine phosphatase LAR promotes R7 photoreceptor axon targeting by a phosphatase-independent signaling mechanism
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The receptor protein tyrosine phosphatase LAR promotes R7 photoreceptor axon targeting by a phosphatase-independent signaling mechanism

机译：受体蛋白酪氨酸磷酸酶LAR通过不依赖磷酸酶的信号传导机制促进R7感光轴突靶向

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摘要

Receptor protein tyrosine phosphatases (RPTPs) control many aspects of nervous system development. At the Drosophila neu-romuscular junction (NMJ), regulation of synapse growth and maturation by the RPTP LAR depends on catalytic phosphatase activity and on the extracellular ligands Syndecan and Dally-like. We show here that the function of LAR in controlling R7 photo-receptor axon targeting in the visual system differs in several respects. The extracellular domain of LAR important for this process is distinct from the domains known to bind Syndecan and Dally-like, suggesting the involvement of a different ligand. R7 targeting does not require LAR phosphatase activity, but instead depends on the phosphatase activity of another RPTP, PTP69D. In addition, a mutation that prevents dimerization of the intracellular domain of LAR interferes with its ability to promote R7 targeting, although it does not disrupt phosphatase activity or neuromuscu-lar synapse growth. We propose that LAR function in R7 is independent of its phosphatase activity, but requires structural features that allow dimerization and may promote the assembly of downstream effectors.
机译：受体蛋白酪氨酸磷酸酶（RPTP）控制神经系统发育的许多方面。在果蝇中性核连接处（NMJ），RPTP LAR对突触生长和成熟的调节取决于催化磷酸酶的活性以及胞外配体Syndecan和Dally-like。我们在这里显示LAR在视觉系统中控制R7感光轴突靶向的功能在几个方面有所不同。对于该过程重要的LAR的胞外域与已知与Syndecan和Dally样结合的域不同，这表明存在不同的配体。 R7靶向不需要LAR磷酸酶活性，而是取决于另一个RPTP PTP69D的磷酸酶活性。此外，阻止LAR细胞内结构域二聚化的突变会干扰其促进R7靶向的能力，尽管它不会破坏磷酸酶的活性或神经肌肉突触的生长。我们建议R7中的LAR功能独立于其磷酸酶活性，但需要允许二聚化并可能促进下游效应子装配的结构特征。

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