Multivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains of the SUMO | Zendy

Kirstin Keusekotten | Zendy; Veronika N. Bade | Zendy; Katrin Meyer-Teschendorf | Zendy; Annie M. Sriramachandran | Zendy; Katrin Fischer | Zendy; Anke Krause | Zendy; Christiane Horst | Zendy; Günter Schwarz | Zendy; Kay Hofmann | Zendy; R. Jürgen Dohmen | Zendy; Gerrit J. K. Praefcke | Zendy

Open Access

Multivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains of the SUMO

Author(s) -

Kirstin Keusekotten,

Veronika N. Bade,

Katrin Meyer-Teschendorf,

Annie M. Sriramachandran,

Katrin Fischer,

Anke Krause,

Christiane Horst,

Günter Schwarz,

Kay Hofmann,

R. Jürgen Dohmen,

Gerrit J. K. Praefcke

Publication year - 2013

Publication title -

biochemical journal

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.706

H-Index - 265

eISSN - 1470-8728

pISSN - 0264-6021

DOI - 10.1042/bj20130753

Subject(s) - rnf4 , ubiquitin ligase , ubiquitin , sumo protein , zinc finger , dna , ring finger domain , ring finger , nuclear protein , biology , dna ligase , microbiology and biotechnology , chemistry , biochemistry , computational biology , genetics , transcription factor , gene

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.

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