Moonlighting glyceraldehyde-3-phosphate dehydrogenase: posttranslational modification, protein and nucleic acid interactions in normal cells and in human pathology

被引：23

作者：

Sirover, Michael A. ^{[1
]}

机构：

[1] Temple Univ, Lewis Katz Sch Med, Dept Pharmacol, 3240 North Broad St, Philadelphia, PA 19140 USA

来源：

CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY | 2020年 / 55卷 / 04期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

Glyceraldehyde-3-phosphate dehydrogenase; moonlighting protein; posttranslational modification; mRNA stability; DNA structure; URACIL DNA-GLYCOSYLASE; MESSENGER-RNA STABILITY; OVARIAN-CANCER CELLS; ALZHEIMERS-DISEASE; POSTTRANSCRIPTIONAL REGULATION; ENDOTHELIN-1; EXPRESSION; 3'-UNTRANSLATED REGION; PHYSICAL ASSOCIATION; BINDING PROTEINS; POLYMERASE-II;

D O I：

10.1080/10409238.2020.1787325

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：

Moonlighting glyceraldehyde-3-phosphate dehydrogenase (GAPDH) exhibits multiple functions separate and distinct from its historic role in energy production. Further, it exhibits dynamic changes in its subcellular localization which is an a priori requirement for its multiple activities. Separately, moonlighting GAPDH may function in the pathology of human disease, involved in tumorigenesis, diabetes, and age-related neurodegenerative disorders. It is suggested that moonlighting GAPDH function may be related to specific modifications of its protein structure as well as the formation of GAPDH protein: protein or GAPDH protein: nucleic acid complexes.

引用

页码：354 / 371

页数：18

共 77 条

[31] Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase [J].