Spatiotemporal analysis of the molecular interaction between PICK1 and PKC
Spatiotemporal analysis of the molecular interaction between PICK1 and PKC
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DOI：
10.1267/ahc.06025
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发表时间：
2006-01-01
影响因子：
2.4
通讯作者：
Saito, Naoaki
中科院分区：
文献类型：
--
作者：
Masukawa, Kenji;Sakai, Norio;Saito, Naoaki
PICK 1是最初使用酵母双杂交系统鉴定为蛋白激酶C α（α PKC）结合蛋白的蛋白质。除了α PKC，PICK 1复合物结合并调节各种跨膜蛋白，包括受体和转运蛋白。然而，PICK 1何时以及在何处与α PKC结合尚未阐明。我们使用实时成像技术研究了PICK 1和PKC的时空相互作用，并显示激活的α PKC与PICK 1结合并将其转运到质膜。虽然PICK 1的膜转位需要激活α PKC，但即使在PKC移回细胞质后，PICK 1仍保留在膜上。这些结果表明，α PKC和PICK 1之间的相互作用是短暂的，并且可能不是PICK 1或膜上α PKC调节受体/转运蛋白所必需的。
PICK1 is a protein which was initially identified as a protein kinase C alpha (alpha PKC) binding protein using the yeast two-hybrid system. In addition to alpha PKC, the PICK1 complex binds to and regulates various transmembrane proteins including receptors and transporters. However, it has not been clarified when and where PICK1 binds to alpha PKC. We examined the spatio-temporal interaction of PICK1 and PKC using live imaging techniques and showed that the activated alpha PKC binds to PICK1 and transports it to the plasma membrane. Although the membrane translocation of PICK1 requires the activation of alpha PKC, PICK1 is retained on the membrane even after PKC moves back to the cytosol. These results suggest that the interaction between alpha PKC and PICK1 is transient and may not be necessary for the regulation of receptors/transporters by PICK1 or by alpha PKC on the membrane.