Protein processing:

FEBS Letters

Brooks, Doug A¹ 

[1] Lysosomal Diseases Research Unit, Department of Chemical Pathology, Women's and Children's Hospital, North Adelaide, S.A. 5006, Australia

关键词: Protein processing;    Folding;    Mutation;    Molecular chaperone;    Genetic disease;    Endoplasmic reticulum;    Protein degradation;    Pathophysiology;   

DOI  :  10.1016/S0014-5793(97)00423-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Genetic diseases associated with an enzyme deficiency frequently have reduced intracellular levels of the mutant protein, despite apparently normal levels of message and protein synthesis. It has been suggested that the endoplasmic reticulum (ER) can recognise mutant protein as incorrectly folded and invoke ‘quality control’ processes which cause the retention and degradation of this protein. This process may occur, even for mutations which do not abrogate protein activity, contributing directly to pathophysiology. Genetic diseases associated with defects in ER and Golgi processing proteins have also been reported and generally result in impaired processing of multiple protein products. In this review the role of the ER and Golgi in the pathogenesis of genetic diseases relating to the vacuolar network are discussed.

【 授权许可】

Unknown