Sorkin Alexander
Department of Pharmacology, University of Colorado Health Sciences Center, Aurora, Colorado 80045-3649, USA.
Sci STKE. 2005 Jan 18;2005(267):pe1. doi: 10.1126/stke.2672005pe1.
The subcellular localization of transmembrane receptors and other signaling proteins has emerged as a key component in the regulation of the intensity and specificity of their activity. Recent research indicates that immature TrkA neurotrophin receptors are transactivated in the Golgi apparatus after stimulation of neuropeptide pituitary adenylate cyclase-activating polypeptide PAC1 receptors or adenosine A(2A) receptors. Transactivation occurs independently of the TrkA extracellular ligand, nerve growth factor (NGF), through a signaling pathway that is distinct from that used in the transactivation of other receptor tyrosine kinases and has consequences distinct from those elicited by NGF at the plasma membrane.
跨膜受体和其他信号蛋白的亚细胞定位已成为调节其活性强度和特异性的关键组成部分。最近的研究表明,在神经肽垂体腺苷酸环化酶激活多肽PAC1受体或腺苷A(2A)受体受到刺激后,未成熟的TrkA神经营养因子受体在高尔基体中被反式激活。反式激活独立于TrkA细胞外配体神经生长因子(NGF)发生,通过一条不同于其他受体酪氨酸激酶反式激活所使用的信号通路,并且产生与NGF在质膜上引发的后果不同的后果。