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spinqualitylabelsall models Human spindlin-1 (green) complex with histone H3 peptide (grey) containing trimethyl lysine, MPD, Mg+2 (green) and Cl- (green) ions (PDB code 4mzg) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Spindlin-1 (SPIN1) is a Tudor-like domain-containing protein is a histone methylation effector protein and facilitates the expression of rRNA genes[1]. SPIN1 senses a cis-tail histone H3 methylation pattern. Spindlin-2B is involved in the regulation of cell cycle progression. Relevance SPIN1 is implicated in liposarcoma and its inhibitors may represent a novel therapeutic strategy[2]. Structural highlights The crystal complex of SPIN1 and histone H3 peptide shows the encapsulation of the histone trimethyllysine and its Arg in hydrophobic pockets of SPIN1[3].

3D Structures of spindlin

Updated on 16-January-2018

References

1. ↑ Wang W, Chen Z, Mao Z, Zhang H, Ding X, Chen S, Zhang X, Xu R, Zhu B. Nucleolar protein Spindlin1 recognizes H3K4 methylation and stimulates the expression of rRNA genes. EMBO Rep. 2011 Oct 28;12(11):1160-6. doi: 10.1038/embor.2011.184. PMID:21960006 doi:http://dx.doi.org/10.1038/embor.2011.184
2. ↑ Franz H, Greschik H, Willmann D, Ozretic L, Jilg CA, Wardelmann E, Jung M, Buettner R, Schule R. The histone code reader SPIN1 controls RET signaling in liposarcoma. Oncotarget. 2015 Mar 10;6(7):4773-89. doi: 10.18632/oncotarget.3000. PMID:25749382 doi:http://dx.doi.org/10.18632/oncotarget.3000
3. ↑ Su X, Zhu G, Ding X, Lee SY, Dou Y, Zhu B, Wu W, Li H. Molecular basis underlying histone H3 lysine-arginine methylation pattern readout by Spin/Ssty repeats of Spindlin1. Genes Dev. 2014 Mar 15;28(6):622-36. doi: 10.1101/gad.233239.113. Epub 2014 Mar, 3. PMID:24589551 doi:http://dx.doi.org/10.1101/gad.233239.113