Abstract
RNF4 (RING finger protein 4) is a STUbL [SUMO (small ubiquitin-related modifier)-targeted ubiquitin ligase] controlling PML (promyelocytic leukaemia) nuclear bodies, DNA double strand break repair and other nuclear functions. In the present paper, we describe that the sequence and spacing of the SIMs (SUMO-interaction motifs) in RNF4 regulate the avidity-driven recognition of substrate proteins carrying SUMO chains of variable length.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Binding Sites
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HeLa Cells
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Humans
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Molecular Sequence Data
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Nuclear Proteins / chemistry*
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Nuclear Proteins / metabolism*
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Protein Binding / physiology
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Protein Interaction Domains and Motifs* / physiology
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SUMO-1 Protein / metabolism*
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Saccharomyces cerevisiae
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Substrate Specificity
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Sumoylation / physiology*
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Transcription Factors / chemistry*
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Transcription Factors / metabolism*
Substances
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Nuclear Proteins
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RNF4 protein, human
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SUMO-1 Protein
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Transcription Factors