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

被引：22
|
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：
美国国家科学基金会; 美国国家卫生研究院;
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
收藏
页码：354 / 371
页数：18
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