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III类β-微管蛋白的翻译后修饰

Posttranslational modification of class III beta-tubulin.

作者信息

Lee M K, Rebhun L I, Frankfurter A

机构信息

Department of Biology, University of Virginia, Charlottesville 22901.

出版信息

Proc Natl Acad Sci U S A. 1990 Sep;87(18):7195-9. doi: 10.1073/pnas.87.18.7195.

DOI:10.1073/pnas.87.18.7195
PMID:2402501
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC54710/
Abstract

The charge heterogeneity of class III beta-tubulin (beta III) during neural development was analyzed by high-resolution isoelectric focusing/two-dimensional polyacrylamide gel electrophoresis in combination with site-specific proteolytic digestion and immunological detection. The number of beta III isoforms (charge variants) gradually increases from one in embryonic brain to seven in adult brain. All of the charge heterogeneity is due to posttranslationally modified sites located within the extreme C-terminal region of the beta III polypeptide. One beta III isoform is present in testis, the only other tissue in which this isotype is expressed. The testis beta III isoform cofocuses with the earliest-appearing embryonic brain beta III charge variant. Our results indicate that the posttranslational modifications of beta III are developmentally regulated, occur at more than one site, and are neuron-specific. The location of these modifications within the extreme C-terminal domain suggests that their function is to modulate the interaction of tubulin with microtubule-associated proteins.

摘要

通过高分辨率等电聚焦/二维聚丙烯酰胺凝胶电泳结合位点特异性蛋白水解消化和免疫检测，分析了神经发育过程中III类β微管蛋白（βIII）的电荷异质性。βIII同工型（电荷变体）的数量从胚胎脑中的一种逐渐增加到成体脑中的七种。所有电荷异质性均归因于位于βIII多肽极端C末端区域内的翻译后修饰位点。一种βIII同工型存在于睾丸中，这是表达这种同型的唯一其他组织。睾丸βIII同工型与最早出现的胚胎脑βIII电荷变体共聚焦。我们的结果表明，βIII的翻译后修饰受发育调控，发生在多个位点，且具有神经元特异性。这些修饰在极端C末端结构域内的位置表明它们的功能是调节微管蛋白与微管相关蛋白的相互作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/e1854577551d/pnas01043-0279-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/214bd435d4bd/pnas01043-0277-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/c444bcd0daf6/pnas01043-0277-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/a2eb6a970fbc/pnas01043-0278-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/daa5662c2bd6/pnas01043-0278-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/0403e3d8f8bb/pnas01043-0278-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/3ee593e7fc19/pnas01043-0278-d.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/2398dc12cfdb/pnas01043-0279-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/911790f8c266/pnas01043-0279-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/e1854577551d/pnas01043-0279-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/214bd435d4bd/pnas01043-0277-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/c444bcd0daf6/pnas01043-0277-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/a2eb6a970fbc/pnas01043-0278-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/daa5662c2bd6/pnas01043-0278-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/0403e3d8f8bb/pnas01043-0278-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/3ee593e7fc19/pnas01043-0278-d.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/2398dc12cfdb/pnas01043-0279-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/911790f8c266/pnas01043-0279-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60ef/54710/e1854577551d/pnas01043-0279-c.jpg

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