受体酪氨酸激酶的“SLAP”效应：类Src衔接蛋白作为受体酪氨酸激酶信号传导关键因子的新作用
RTK SLAP down: the emerging role of Src-like adaptor protein as a key player in receptor tyrosine kinase signaling.
作者信息
Wybenga-Groot Leanne E, McGlade C Jane
机构信息
The Arthur and Sonia Labatt Brain Tumour Research Centre and Program in Cell Biology, The Hospital for Sick Children, 555 University Avenue, Toronto, ON, Canada, M5G 1X8.
The Arthur and Sonia Labatt Brain Tumour Research Centre and Program in Cell Biology, The Hospital for Sick Children, 555 University Avenue, Toronto, ON, Canada, M5G 1X8; Department of Medical Biophysics, University of Toronto, 610 University Avenue, Toronto, ON, Canada, M5G 2M9.
出版信息
Cell Signal. 2015 Feb;27(2):267-74. doi: 10.1016/j.cellsig.2014.11.010. Epub 2014 Nov 18.
SLAP (Src like adaptor protein) contains adjacent Src homology 3 (SH3) and Src homology 2 (SH2) domains closely related in sequence to that of cytoplasmic Src family tyrosine kinases. Expressed most abundantly in the immune system, SLAP function has been predominantly studied in the context of lymphocyte signaling, where it functions in the Cbl dependent downregulation of antigen receptor signaling. However, accumulating evidence suggests that SLAP plays a role in the regulation of a broad range of membrane receptors including members of the receptor tyrosine kinase (RTK) family. In this review we highlight the role of SLAP in the ubiquitin dependent regulation of type III RTKs PDGFR, CSF-1R, KIT and Flt3, as well as Eph family RTKs. SLAP appears to bind activated type III and Eph RTKs via a conserved autophosphorylated juxtamembrane tyrosine motif in an SH2-dependent manner, suggesting that SLAP is important in regulating RTK signaling.
Src样衔接蛋白（SLAP）含有相邻的Src同源结构域3（SH3）和Src同源结构域2（SH2），其序列与细胞质Src家族酪氨酸激酶的序列密切相关。SLAP在免疫系统中表达最为丰富，其功能主要在淋巴细胞信号传导的背景下进行研究，在那里它在Cbl依赖的抗原受体信号下调中发挥作用。然而，越来越多的证据表明，SLAP在包括受体酪氨酸激酶（RTK）家族成员在内的广泛膜受体的调节中发挥作用。在这篇综述中，我们强调了SLAP在泛素依赖性调节III型RTK（血小板衍生生长因子受体，CSF-1R，KIT和Flt3）以及Eph家族RTK中的作用。SLAP似乎通过保守的自磷酸化近膜酪氨酸基序以SH2依赖性方式结合活化的III型和Eph RTK，这表明SLAP在调节RTK信号传导中很重要。
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