Function
Spindlin-1 (SPIN1) is a Tudor-like domain-containing protein which 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.
- Spindlin-4 binds trimethylated histone H3K4[2].
Relevance
SPIN1 is implicated in liposarcoma and its inhibitors may represent a novel therapeutic strategy[3].
Structural highlights
The crystal complex of SPIN1 and histone H3 peptide shows the and in hydrophobic pockets of SPIN1[4].
3D Structures of spindlin
Updated on 14-August-2024
References
- ↑ 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
- ↑ Zhang X, Thielert M, Li H, Cravatt BF. SPIN4 Is a Principal Endogenous Substrate of the E3 Ubiquitin Ligase DCAF16. Biochemistry. 2021 Mar 9;60(9):637-642. PMID:33636084 doi:10.1021/acs.biochem.1c00067
- ↑ 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
- ↑ 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
