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Portland Press, Biochemical Journal, 1(457), p. 207-214, 2013

DOI: 10.1042/bj20130753

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

Journal article published in 2013 by Kirstin Keusekotten, Veronika N. Bade, Katrin Meyer-Teschendorf, Annie Miriam Sriramachandran, Katrin Fischer-Schrader, Anke Krause, Christiane Horst, Günter Schwarz, Kay Hofmann, R. Jürgen Dohmen, R. Jürgen Dohmen, Gerrit J. K. Praefcke
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.