期刊
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES
卷 786, 期 1-2, 页码 311-318出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S1570-0232(02)00743-2
关键词
beta-tubulin; GST fusion protein; myelin basic protein; P2X receptor isoforms
To isolate proteins interacting with P2X receptors, GST fusion proteins containing the intracellular C terminal tail of P2X(2), P2X(5), or P2X(7) were used as bait to screen detergent extracts of rat brain synaptosomes. By SDS-PAGE combined with mass spectrometry, two interacting proteins were identified: betaPIII tubulin and myelin basic protein. While myelin basic protein bound to all three P2X subunits, betaIII tubulin interacted exclusively with the P2X(2) subunit. The tubulin binding domain could be confined to a proline-rich segment (amino acids 371-412) of the P2X(2) subunit. Our results suggest a role for microtubules in the cellular localisation of the P2X(2) receptor. (C) 2002 Elsevier Science B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据