Signal regulatory protein alpha (SIRPalpha)/CD47 interaction and function.

Signal regulatory protein alpha (SIRPalpha)/CD47 interaction and function.
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DOI:
10.1016/j.coi.2009.01.008
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发表时间:
2009-02
影响因子:
7
通讯作者:
Barclay AN
Barclay AN
中科院分区:
医学2区
文献类型:
--
作者:
Barclay AN

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SIRPα 是一种存在于骨髓细胞上的抑制性受体,与广泛分布的膜蛋白 CD47 相互作用。激活成员 SIRPβ 尽管在细胞外区域与 SIRPα 具有广泛的序列相似性,但与 CD47 的结合可以忽略不计。 SIRPα / CD47 相互作用是不寻常的,因为它可以通过 SIRPα 和 CD47 产生双向信号传导。这篇综述集中于 SIRPα 与 CD47 的相互作用,其中最近的数据揭示了蛋白质的结构,包括确定为什么激活的 SIRPβ 不结合 CD47、广泛多态性的证据以及该蛋白质和配对受体的进化和功能的含义。这种相互作用可以通过受体的内吞作用、蛋白水解作用以及表面活性剂蛋白的相互作用来改变。
SIRPα is an inhibitory receptor present on myeloid cells that interacts with a widely distributed membrane protein CD47. The activating member SIRPβ, despite extensive sequence similarity to SIRPα in the extracellular region, shows negligible binding to CD47. The SIRPα / CD47 interaction is unusual in that it can lead to bidirectional signalling through both SIRPα and CD47. This review concentrates on the interactions of SIRPα with CD47 where recent data have shed light on the structure of the proteins including determining why the activating SIRPβ does not bind CD47, evidence of extensive polymorphisms and implication for the evolution and function of this protein and paired receptors in general. The interaction may be modified by endocytosis of the receptors, cleavage by proteolysis and through interactions of surfactant proteins.
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