Tailoring of Membrane Proteins by Alternative Splicing of Pre-mRNA

被引：24

作者：

Mittendorf, Kathleen F. ^{[1
,2
]}

Deatherage, Catherine L. ^{[1
,2
]}

Ohi, Melanie D. ^{[2
,3
]}

Sanders, Charles R. ^{[1
,2
]}

机构：

[1] Vanderbilt Univ, Sch Med, Dept Biochem, Nashville, TN 37232 USA

[2] Vanderbilt Univ, Struct Biol Ctr, Sch Med, Nashville, TN 37232 USA

[3] Vanderbilt Univ, Dept Cellular & Dev Biol, Sch Med, Nashville, TN 37232 USA

来源：

BIOCHEMISTRY | 2012年 / 51卷 / 28期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

AMYLOID PRECURSOR PROTEIN; TISSUE-SPECIFIC EXPRESSION; MUSCLE RYANODINE RECEPTOR; GAMMA-SECRETASE ACTIVITY; CLEAVING ENZYME BACE; UNSTABLE CTG REPEAT; ALZHEIMERS-DISEASE; BETA-SECRETASE; SECONDARY STRUCTURE; 5-HT4; RECEPTORS;

D O I：

10.1021/bi3007065

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Alternative splicing (AS) of RNA is a key mechanism for diversification of the eukaryotic proteome. In this process, different mRNA transcripts can be produced through altered excision and/or inclusion of exons during processing of the pre-mRNA molecule. Since its discovery, AS has been shown to play roles in protein structure, function, and localization. Dysregulation of this process can result in disease phenotypes. Moreover, AS pathways are promising therapeutic targets for a number of diseases. Integral membrane proteins (MPs) represent a class of proteins that may be particularly amenable to regulation by alternative splicing because of the distinctive topological restraints associated with their folding, structure, trafficking, and function. Here, we review the impact of AS on MP form and function and the roles of AS in MP-related disorders such as Alzheimer's disease.

引用

页码：5541 / 5556

页数：16

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