Decoding the SUMO signal

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    Abstract

    SUMO (small ubiquitin-like modifier) emerged from the shadow of the well-established ubiquitin some 15 years ago when it was shown that a distinct conjugation pathway was responsible for SUMO modification. Since then it has been established that SUMO modifies over a thousand substrates and plays diverse roles in many important biological processes. Recognition of SUMO is mediated by short peptide sequences known as SIMs (SUMO-interaction motifs) that allow effector proteins to engage SUMO-modified substrates. Like ubiquitin, SUMO can form polymeric chains, and these chains can be recognized by proteins containing multiple SIMs. One protein that contains such a sequence of SIMs also contains a RING (really interesting new gene) domain that is the hallmark of a ubiquitin E3 ligase. This ubiquitin ligase known as RNF4 (RING finger protein 4) has the unique property that it can recognize SUMO-modified proteins and target them for ubiquitin-mediated proteolysis. Structural and biochemical analyses of RNF4 has shed light on the long sought after mechanism of ubiquitin transfer and illustrates how its RING domain primes the ubiquitin-loaded E2 for catalysis.

    Original languageEnglish
    Pages (from-to)463-473
    Number of pages11
    JournalBiochemical Society Transactions
    Volume41
    Issue number2
    DOIs
    Publication statusPublished - Apr 2013

    Keywords

    • ACUTE PROMYELOCYTIC LEUKEMIA
    • UBIQUITIN E3 LIGASE
    • TRANSCRIPTION FACTOR
    • PML NUCLEAR-BODIES
    • CONJUGATING ENZYME
    • E3 ligase
    • ubiquitin
    • DNA damage
    • small ubiquitin-like modifier (SUMO)
    • RAR-ALPHA
    • MODIFIER SUMO
    • RING finger protein 4 (RNF4)
    • DNA-DAMAGE RESPONSE
    • PORE COMPLEX
    • really interesting new gene (RING)
    • BINDING MOTIF

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