SUMO junction—what's your function?

Kerscher, Oliver

doi:10.1038/sj.embor.7400980

Cited by 366 publications

(289 citation statements)

References 46 publications

(85 reference statements)

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“…Recently it has been reported that several proteins including PML could interact with SUMO molecules non-covalently through a SUMO interacting motif (SIM) (Minty et al 2000;Song et al 2004;Shen et al 2006;Kerscher 2007). However, no SIM could be identified in BCL11A within the range of our search.…”

Section: Discussionmentioning

confidence: 50%

BCL11A is a SUMOylated protein and recruits SUMO‐conjugation enzymes in its nuclear body

Kuwata

Nakamura

2008

Genes to Cells

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BCL11A/EVI9 is a zinc‐finger protein predominantly expressed in brain and hematopoietic cells. Previous studies show that BCL11A is involved in acute myelomonocytic leukemia and chronic lymphoid leukemia in mouse and human, respectively. Moreover, BCL11A is localized in the characteristic nuclear body in which BCL6 is co‐localized. However, the significance of BCL11A in leukemogenesis and nuclear function remains unknown. In this study we show that BCL11A interacts with UBC9, a small ubiquitin‐like modifier (SUMO) E2 conjugating enzyme, and recruits SUMO1 into the nuclear body. A lysine residue at amino acid 634 of BCL11A is SUMOylated but not required for the SUMO1 recruitment. The N‐terminal region of BCL11A is responsible for SUMO1 recruitment as well as its nuclear body formation. We also show that SENP2, a SUMO specific peptidase, is co‐localized in the nuclear body. These results suggest that BCL11A could be involved in the SUMO conjugation system, and that BCL11A might play an important role in protein modification.

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Section: Discussionmentioning

confidence: 50%

BCL11A is a SUMOylated protein and recruits SUMO‐conjugation enzymes in its nuclear body

Kuwata

Nakamura

2008

Genes to Cells

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“…Based on our observations, we can infer the existence of a mechanisms that controls nucleolar localization of a subset of given nuclear proteins by their targeting to the nucleolus via transient polysumoylation and their nucleolar retention via recognition by some SUMO-binding protein(s) residing in the nucleolus. As putative SUMObinding domains have recently been identified (Hecker et al 2006;Lin et al 2006;Kerscher 2007;Sun et al 2007;Uzunova 2007), it is conceivable that some nucleolar proteins may have an ability to serve as receptors for sumoylated proteins, which hence acquire a nucleolarspecific function through such interactions. The experimental approach to modeling polysumoylation in vivo.…”

Section: Discussionmentioning

confidence: 99%

In vivo modeling of polysumoylation uncovers targeting of Topoisomerase II to the nucleolus via optimal level of SUMO modification

Takahashi

Strunnikov

2007

Chromosoma

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Conjugation of SUMO to target proteins is an essential eukaryotic regulatory pathway. Multiple potential SUMO substrates were identified among nuclear and chromatin proteins by proteomic approaches. However, the functional roles of SUMO-modified pools of individual proteins remain largely obscure, as only a small fraction of a given target is sumoylated and therefore is experimentally inaccessible. To overcome this technical difficulty in case of Topoisomerase II, we employed constitutive SUMO modification, enabling tracking of modified Top2p, not only biochemically but also cytologically and genetically. Top-oisomerase II fused to a critical number of SUMO repeats is concentrated at the specific intranuclear domain, the nucleolus, when more than four SUMO moieties are added, indicating that fused SUMO repeats are biologically active. Further analysis has established that poly-sumoylation of Top2p is required for the stable maintenance of the nucleolar organizer, linking SUMO-mediated targeting to functional maintenance of ribosomal RNA gene cluster.

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“…This led to the identification of a large number of covalently modified targets (8)(9)(10)(11)(12). However, SUMO also interacts with proteins noncovalently (13). Because only a few SUMO-interacting proteins (SIPs) have been identified in yeast and metazoans (14)(15)(16)(17)(18) and none has been identified in plants so far, the extent and significance of noncovalent SUMO interactions is still poorly understood.…”

mentioning

confidence: 99%

Identification of Arabidopsis SUMO-interacting proteins that regulate chromatin activity and developmental transitions

Elrouby

Bonequi

Porri

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Posttranslational modification of proteins by small ubiquitin-like modifier (SUMO) plays essential roles in eukaryotic growth and development. Many covalently modified SUMO targets have been identified; however, the extent and significance of noncovalent interactions of SUMO with cellular proteins is poorly understood. Here, large-scale yeast two-hybrid screens repeatedly identified a surprisingly small number of proteins that interacted with three Arabidopsis SUMO isoforms. These SUMO-interacting proteins are nuclear and fall into two main categories: six histone or DNA methyltransferses or demethylases and six proteins that we show to be the evolutionary and functional homologs of SUMOtargeted ubiquitin ligases (STUbLs). The selectivity of the screen for several methylases and demethylases suggests that SUMO interaction with these proteins has a significant impact on chromatin methylation. Furthermore, the Arabidopsis STUbLs (AT-STUbLs) complemented to varying degrees the growth defects of the Schizosaccharomyces pombe STUbL mutant rfp1/rfp2, and three of them also complemented the genome integrity defects of this mutant, demonstrating that these proteins show STUbL activity. We show that one of the AT-STUbLs least related to the S. pombe protein, AT-STUbL4, has acquired a plant-specific function in the floral transition. It reduces protein levels of CYCLING DOF FACTOR 2, hence increasing transcript levels of CONSTANS and promoting flowering through the photoperiodic pathway.SIM | Slx5/Slx8 | Nucleolus | Flowering time | CDF

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SUMO junction—what's your function?

Cited by 366 publications

References 46 publications

BCL11A is a SUMOylated protein and recruits SUMO‐conjugation enzymes in its nuclear body

BCL11A is a SUMOylated protein and recruits SUMO‐conjugation enzymes in its nuclear body

In vivo modeling of polysumoylation uncovers targeting of Topoisomerase II to the nucleolus via optimal level of SUMO modification

Identification of Arabidopsis SUMO-interacting proteins that regulate chromatin activity and developmental transitions

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