Integral membrane proteins in proteomics. How to break open the black box?

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• 作者：O. Vit ; ^{ondrvit@gmail.com} ; J. Petrak
• 关键词：Integral membrane proteins ; Detergent removal ; Transmembrane ; Surfaceomics ; Alternative proteases ; Cyanogen bromide
• 刊名：Journal of Proteomics
• 出版年：2017
• 出版时间：5 February 2017
• 年：2017
• 卷：153
• 期：Complete
• 页码：8-20
• 全文大小：1091 K
• 卷排序：153

文摘

Integral membrane proteins (IMPs) are coded by 20–30% of human genes and execute important functions – transmembrane transport, signal transduction, cell-cell communication, cell adhesion to the extracellular matrix, and many other processes. Due to their hydrophobicity, low expression and lack of trypsin cleavage sites in their transmembrane segments, IMPs have been generally under-represented in routine proteomic analyses. However, the field of membrane proteomics has changed markedly in the past decade, namely due to the introduction of filter assisted sample preparation (FASP), the establishment of cell surface capture (CSC) protocols, and the development of methods that enable analysis of the hydrophobic transmembrane segments. This review will summarize the recent developments in the field and outline the most successful strategies for the analysis of integral membrane proteins.SignificanceIntegral membrane proteins (IMPs) are attractive therapeutic targets mostly due to their many important functions. However, our knowledge of the membrane proteome is severely limited to effectively exploit their potential. This is mostly due to the lack of appropriate techniques or methods compatible with the typical features of IMPs, namely hydrophobicity, low expression and lack of trypsin cleavage sites. This review summarizes the most recent development in membrane proteomics and outlines the most successful strategies for their large-scale analysis.