Multivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains of the SUMO.
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ABSTRACT:
SUBMITTER: Keusekotten K
PROVIDER: S-EPMC3901395 | biostudies-literature | 2014 Jan
REPOSITORIES: biostudies-literature
Publications
Multivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains of the SUMO.
Keusekotten Kirstin K Bade Veronika N VN Meyer-Teschendorf Katrin K Sriramachandran Annie Miriam AM Fischer-Schrader Katrin K Krause Anke A Horst Christiane C Schwarz Günter G Hofmann Kay K Dohmen R Jürgen RJ Praefcke Gerrit J K GJ
The Biochemical journal 20140101 1
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. ...[more]
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