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Ubiquitin Lys 63 chains - second-most abundant, but poorly understood in plants.

ABSTRACT: Covalent attachment of the small modifier ubiquitin to Lys ?-amino groups of proteins is surprisingly diverse. Once attached to a substrate, ubiquitin is itself frequently modified by ubiquitin, to form chains. All seven Lys residues of ubiquitin, as well as its N-terminal Met, can be ubiquitylated, implying cellular occurrence of different ubiquitin chain types. The available data suggest that the synthesis, recognition, and hydrolysis of different chain types are precisely regulated. This remarkable extent of control underlies a versatile cellular response to substrate ubiquitylation. In this review, we focus on roles of Lys63-linked ubiquitin chains in plants. Despite limited available knowledge, several recent findings illustrate the importance of these chains as signaling components in plants.

SUBMITTER: Tomanov K

PROVIDER: S-EPMC3907715 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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Ubiquitin Lys 63 chains - second-most abundant, but poorly understood in plants.

Tomanov Konstantin K Luschnig Christian C Bachmair Andreas A

Frontiers in plant science 20140131

Covalent attachment of the small modifier ubiquitin to Lys ε-amino groups of proteins is surprisingly diverse. Once attached to a substrate, ubiquitin is itself frequently modified by ubiquitin, to form chains. All seven Lys residues of ubiquitin, as well as its N-terminal Met, can be ubiquitylated, implying cellular occurrence of different ubiquitin chain types. The available data suggest that the synthesis, recognition, and hydrolysis of different chain types are precisely regulated. This rema ...[more]

PMID: 24550925

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