Role of the SUMO-interacting motif in HIPK2 targeting to the PML nuclear bodies and regulation of p53

Sung, Kyung Rim; Lee, Yun-Ah; Kim, Eui‐Tae; Lee, Seung-Rock; Ahn, Jin-Hyun; Choi, Cheol Yong

doi:10.1016/j.yexcr.2010.12.016

Cited by 42 publications

(38 citation statements)

References 48 publications

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“…For example, PML-NBs are formed by association of SUMO modified PML with proteins containing SIMs including PML [36], Daxx [37], TDG [38], RNF4 [39]–[41], and HIPK2 [42]. Consistent with SUMO binding being required for localization of these proteins to PML-NBs, we found that the MYM-type zinc fingers in ZNF198 were also necessary but not sufficient for localization to PML-NBs.…”

Section: Discussionsupporting

confidence: 54%

Characterization of the SUMO-Binding Activity of the Myeloproliferative and Mental Retardation (MYM)-Type Zinc Fingers in ZNF261 and ZNF198

et al. 2014

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SUMO-binding proteins interact with SUMO modified proteins to mediate a wide range of functional consequences. Here, we report the identification of a new SUMO-binding protein, ZNF261. Four human proteins including ZNF261, ZNF198, ZNF262, and ZNF258 contain a stretch of tandem zinc fingers called myeloproliferative and mental retardation (MYM)-type zinc fingers. We demonstrated that MYM-type zinc fingers from ZNF261 and ZNF198 are necessary and sufficient for SUMO-binding and that individual MYM-type zinc fingers function as SUMO-interacting motifs (SIMs). Our binding studies revealed that the MYM-type zinc fingers from ZNF261 and ZNF198 interact with the same surface on SUMO-2 recognized by the archetypal consensus SIM. We also present evidence that MYM-type zinc fingers in ZNF261 contain zinc, but that zinc is not required for SUMO-binding. Immunofluorescence microscopy studies using truncated fragments of ZNF198 revealed that MYM-type zinc fingers of ZNF198 are necessary for localization to PML-nuclear bodies (PML-NBs). In summary, our studies have identified and characterized the SUMO-binding activity of the MYM-type zinc fingers in ZNF261 and ZNF198.

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Section: Discussionsupporting

confidence: 54%

Characterization of the SUMO-Binding Activity of the Myeloproliferative and Mental Retardation (MYM)-Type Zinc Fingers in ZNF261 and ZNF198

et al. 2014

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“…Several proteins that are found in PML-NBs contain a phospho-SIM similar to the one found in PML ( Figure S1B; Cho et al, 2009;Lin et al, 2006;Rasheed et al, 2002;Sung et al, 2011). In the case of Daxx, it has been shown that phosphorylation of two serine residues in its phosphoSIM motif increases its binding affinity to SUMO1 and plays a key role in regulating a number of its biologic functions (Chang et al, 2011).…”

Section: Structure Of the Sumo1:daxx-sim-po 4 Complexmentioning

confidence: 80%

“…The best-characterized interactions involving SIMs and either SUMO proteins or SUMOylated proteins occurs during promyelocytic leukemia (PML)-dependent recruitment of proteins into subnuclear structures known as PML-nuclear bodies (PMLNBs) (Cho et al, 2009;Ishov et al, 1999;Lin et al, 2006;Rasheed et al, 2002;Sung et al, 2011). PML is implicated in regulating a wide range of biological processes, including transcription, cell cycle control, and genome integrity (Dellaire and Bazett-Jones, 2007;Salomoni et al, 2012;Zhong et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

“…Like PML, a number of other proteins that transit into PMLNBs, including Daxx and PIAS1, contain a phosphoSIM module, and their noncovalent interaction with SUMO proteins are known to be regulated in a phosphorylation-dependent manner (Cho et al, 2009;Lin et al, 2006;Negorev et al, 2001;Rasheed et al, 2002;Sung et al, 2011). Based on studies analyzing interactions between SUMO proteins and phosphoSIM-containing proteins, it has been postulated that the phosphorylated residues make contacts with positively charged surface residues that are conserved in SUMO family proteins (Chang et al, 2011;Sekiyama et al, 2008;Song et al, 2005;Stehmeier and Muller, 2009;Ullmann et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

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Structural and Functional Characterization of the Phosphorylation-Dependent Interaction between PML and SUMO1

et al. 2015

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PML and several other proteins localizing in PML-nuclear bodies (PML-NB) contain phosphoSIMs (SUMO-interacting motifs), and phosphorylation of this motif plays a key role in their interaction with SUMO family proteins. We examined the role that phosphorylation plays in the binding of the phosphoSIMs of PML and Daxx to SUMO1 at the atomic level. The crystal structures of SUMO1 bound to unphosphorylated and tetraphosphorylated PML-SIM peptides indicate that three phosphoserines directly contact specific positively charged residues of SUMO1. Surprisingly, the crystal structure of SUMO1 bound to a diphosphorylated Daxx-SIM peptide indicate that the hydrophobic residues of the phosphoSIM bind in a manner similar to that seen with PML, but important differences are observed when comparing the phosphorylated residues. Together, the results provide an atomic level description of how specific acetylation patterns within different SUMO family proteins can work together with phosphorylation of phosphoSIM's regions of target proteins to regulate binding specificity.

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“…Deletion of SIM sequence consistently impairs partner NB-association, implying that partner SIM may interact with sumoylated PML to initiate and enforce recruitment. 26,[59][60][61] Indeed, mutation of PML K160 does not interfere with the formation of matrix-associated NB, but completely abrogates partner recruitment. These observations therefore suggest that PML NB assembly is not a stochastic process, but follows an ordered path, which is initiated by an initial seeding (nucleation) step: formation of the PML outer shell (Fig.…”

Section: -51mentioning

confidence: 98%

PML nuclear bodies: Assembly and oxidative stress-sensitive sumoylation

Şahin¹,

Lallemand-Breitenbach²

2014

Nucleus

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Role of the SUMO-interacting motif in HIPK2 targeting to the PML nuclear bodies and regulation of p53

Cited by 42 publications

References 48 publications

Characterization of the SUMO-Binding Activity of the Myeloproliferative and Mental Retardation (MYM)-Type Zinc Fingers in ZNF261 and ZNF198

Characterization of the SUMO-Binding Activity of the Myeloproliferative and Mental Retardation (MYM)-Type Zinc Fingers in ZNF261 and ZNF198

Structural and Functional Characterization of the Phosphorylation-Dependent Interaction between PML and SUMO1

PML nuclear bodies: Assembly and oxidative stress-sensitive sumoylation

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