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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Sonic hedgehog protein signals not as a hydrolytic enzyme but as an apparent ligand for Patched
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Sonic hedgehog protein signals not as a hydrolytic enzyme but as an apparent ligand for Patched

机译：声波刺猬蛋白信号不是水解酶，而是明显的配体

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摘要

The amnino-terminal signaling domain of the Sonic hedgehog secreted protein (Shh-N), which derives from the Shh precursor through an autoprocessing reaction medi- ated by the carboxyl-terminal domain, executes multiple func- tions in embryonic tissue patterning, including induction of ventral and suppression of dorsal cell types in the developing neural tube. An apparent catalytic site within Shh.N is suggested by structural homology to a bacterial carboxypep- tidase. We demonstrate here that alteration of residues pre- sumed to be critical for a hydrolytic activity does not cause a loss of inductive activity, thus ruling out catalysis by Shh-N as a requirement for signaling. We favor the alternative, that hh-N functions primarily as a ligand for the putative recep- tor Patched (Ptc). This possibility is supported by new evi- dence for direct binding of Shh-N to Ptc and by a strong correlation between the affinity of Ptc-binding and the sig- naling potency of Shh-N protein variants carrying alterations of conserved residues in a particular region of the protein surface. These results together suggest that direct Shh-N binding to Ptc is a critical event in transduction of the Shh-N signal.
机译：Sonic刺猬蛋白分泌物（Shh-N）的氨端信号结构域，是通过羧基端结构域介导的自加工反应从Shh前体衍生而来的，它在胚胎组织构图中执行多种功能，包括诱导发育中的神经管腹侧和背侧细胞类型的抑制。与细菌羧肽酶的结构同源性表明，Shh.N中存在明显的催化位点。我们在此证明，据推测对水解活性至关重要的残基改变不会引起诱导活性的损失，因此排除了Shh-N催化作为信号传递的必要条件。我们支持另一种选择，即hh-N主要充当推定的受体修补（Ptc）的配体。 Shh-N与Ptc直接结合的新证据以及Ptc结合的亲和力和携带特定残基的Shh-N蛋白变体的信号强度之间的强相关性支持了这种可能性。蛋白质表面的区域。这些结果共同表明，Shh-N与Ptc的直接结合是Shh-N信号转导中的关键事件。

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