2014Zhongguo shengwu huaxue yu fenzi shengwu xuebaoRequires access

The Role of Neddylation in Tumor Development

Hu Gao

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Abstract

Currently,17 ubiquitin-like proteins( UBLs) have been identified to modify substrates like what the ubiquitin does. UBLs are divided into 9 distinct classes based on the evolutional features,including NEDD8,SUMO,ISG15,FUB1,FAT10,Atg8,Atg12,Urm1,and UFM1. NEDD8 shares the highest amino acid sequence similarity with ubiquitin and is best characterized. Neddylation is a dynamic and reversible post-translational modification,involving covalently binding of NEDD8 to target proteins,or reversiblely,the remove of NEDD8 from modified target proteins. Neddylation plays important roles in the regulation of protein functions,such as conformation change,partner recruitiment and modulation of protein interaction. Recent studies revealed that aberration of neddylation and NEDD8-interacting proteins was significant during tumorigenesis. This review focuses on potential implications of neddylation for the development mechanism of tumor.

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What this paper is about

Currently,17 ubiquitin-like proteins( UBLs) have been identified to modify substrates like what the ubiquitin does. UBLs are divided into 9 distinct classes based on the evolutional features,including NEDD8,SUMO,ISG15,FUB1,FAT10,Atg8,Atg12,Urm1,and UFM1. NEDD8 shares the highest amino acid sequence similarity with ubiquitin and is best characterized. Neddylation is a dynamic and reversible post-translational modification,involving covalently binding of NEDD8 to target proteins,or reversiblely,the remove of NEDD8 from modified target proteins. Neddylation plays important roles in the regulation of protein functions,such as conformation change,partner recruitiment and modulation of protein interaction. Recent studies revealed that aberration of neddylation and NEDD8-interacting proteins was significant during tumorigenesis. This review focuses on potential implications of neddylation for the development mechanism of tumor.

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Available abstract

Currently,17 ubiquitin-like proteins( UBLs) have been identified to modify substrates like what the ubiquitin does. UBLs are divided into 9 distinct classes based on the evolutional features,including NEDD8,SUMO,ISG15,FUB1,FAT10,Atg8,Atg12,Urm1,and UFM1. NEDD8 shares the highest amino acid sequence similarity with ubiquitin and is best characterized. Neddylation is a dynamic and reversible post-translational modification,involving covalently binding of NEDD8 to target proteins,or reversiblely,the remove of NEDD8 from modified target proteins. Neddylation plays important roles in the regulation of protein functions,such as conformation change,partner recruitiment and modulation of protein interaction. Recent studies revealed that aberration of neddylation and NEDD8-interacting proteins was significant during tumorigenesis. This review focuses on potential implications of neddylation for the development mechanism of tumor.

Key concepts: NEDD8, Neddylation, ISG15, Ubiquitin, ATG12, ATG8, Cell biology, Biology

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