Multivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains of the SUMO.
Multivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains of the SUMO.
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DOI：
10.1042/bj20130753
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发表时间：
2014-01-01
期刊：
影响因子：
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通讯作者：
Praefcke GJ
中科院分区：
文献类型：
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作者：
Keusekotten K;Bade VN;Meyer-Teschendorf K;Sriramachandran AM;Fischer-Schrader K;Krause A;Horst C;Schwarz G;Hofmann K;Dohmen RJ;Praefcke GJ
RNF4（RING Finger Protein 4）是一种 STUbL [SUMO（小泛素相关修饰剂）靶向泛素连接酶]，控制 PML（早幼粒细胞白血病）核体、DNA 双链断裂修复和其他核功能。在本文中，我们描述了 RNF4 中 SIM（SUMO 相互作用基序）的序列和间距调节携带可变长度 SUMO 链的底物蛋白的亲和力驱动的识别。如果蛋白质经过 SUMO 链修饰，则泛素连接酶 RNF4 会针对蛋白质进行蛋白酶体降解。 RNF4 通过使用与 SUMO 链非共价相互作用的短肽基序（如果它们包含至少两个 SUMO 部分）来识别其底物。
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. The ubiquitin ligase RNF4 targets proteins for proteasomal degradation if they are modified with SUMO chains. RNF4 recognizes its substrates by using short peptide motifs that interact non-covalently with SUMO chains if they contain at least two SUMO moieties.