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Cell Res. 2006 May;16(5):413-26.

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions.

Author information

1
Department of Plant Pathology and Plant Molecular Biology and Biotechnology Program, The Ohio State University, Columbus, OH 43210, USA. zeng.17@osu.edu

Abstract

Post-translational modification is central to protein stability and to the modulation of protein activity. Various types of protein modification, such as phosphorylation, methylation, acetylation, myristoylation, glycosylation, and ubiquitination, have been reported. Among them, ubiquitination distinguishes itself from others in that most of the ubiquitinated proteins are targeted to the 26S proteasome for degradation. The ubiquitin/26S proteasome system constitutes the major protein degradation pathway in the cell. In recent years, the importance of the ubiquitination machinery in the control of numerous eukaryotic cellular functions has been increasingly appreciated. Increasing number of E3 ubiquitin ligases and their substrates, including a variety of essential cellular regulators have been identified. Studies in the past several years have revealed that the ubiquitination system is important for a broad range of plant developmental processes and responses to abiotic and biotic stresses. This review discusses recent advances in the functional analysis of ubiquitination-associated proteins from plants and pathogens that play important roles in plant-microbe interactions.

PMID:
16699537
DOI:
10.1038/sj.cr.7310053
[Indexed for MEDLINE]
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