Spindlin: Difference between revisions

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<StructureSection load='4mzg' size='350' side='right' caption='Human spindlin-1 (skyblue) complex with histone H3 peptide (wheat) containing trimethyl lysine, MPD, Mg+2 (green) and Cl- (green) ions (PDB code [[4mzg]])' scene='77/778344/Cv/1'>
<StructureSection load='4mzg' size='350' side='right' caption='Human spindlin-1 (skyblue) complex with histone H3 peptide (wheat) containing trimethyl lysine, MPD, Mg+2 (green) and Cl- (green) ions (PDB code [[4mzg]])' scene='77/778344/Cv/1'>
 
__TOC__


== Function ==
== Function ==


'''Spindlin-1''' (SPIN1) is a Tudor-like domain-containing protein is a histone methylation effector protein and facilitates the expression of rRNA genes<ref>PMID:21960006</ref>.  SPIN1 senses a cis-tail histone H3 methylation pattern.  '''Spindlin-2B''' is involved in the regulation of cell cycle progression.
'''Spindlin-1''' (SPIN1) is a Tudor-like domain-containing protein which is a histone methylation effector protein and facilitates the expression of rRNA genes<ref>PMID:21960006</ref>.  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<ref>PMID:33636084</ref>.  


== Relevance ==
== Relevance ==
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== Structural highlights ==
== Structural highlights ==


The crystal complex of SPIN1 and histone H3 peptide shows the <scene name='77/778344/Cv/2'>encapsulation of the histone trimethyllysine</scene> and <scene name='77/778344/Cv/3'>its Arg</scene> in hydrophobic pockets of SPIN1<ref>PMID:24589551</ref>.
The crystal complex of SPIN1 and histone H3 peptide shows the <scene name='77/778344/Cv/4'>encapsulation of the histone trimethyllysine</scene> and <scene name='77/778344/Cv/5'>its Arg</scene> in hydrophobic pockets of SPIN1<ref>PMID:24589551</ref>.
</StructureSection>
 
== 3D Structures of spindlin ==
== 3D Structures of spindlin ==


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**[[2ns2]] – hSPIN1 – human <br />
**[[2ns2]] – hSPIN1 – human <br />
**[[4mzg]], [[4mzh]], [[4mzf]], [[4h75]], [[5y5w]] – hSPIN1 + histone peptide  <br />
**[[4mzg]], [[4mzh]], [[4mzf]], [[4h75]], [[5y5w]], [[7bqz]], [[7bu9]] – hSPIN1 + histone peptide  <br />
**[[5y5w]], [[5jsg]] – hSPIN1 + inhibitor <br />
**[[5jsg]], [[5jsj]], [[6i8b]], [[6i8l]], [[6i8y]], [[6qpl]], [[7ocb]] – hSPIN1 + inhibitor <br />
**[[7e9m]], [[7ea1]] – hSPIN1 + SPIN-DOC <br />
**[[7cna]] – hSPIN1 + SPIN-DOC + inhibitor <br />
**[[8gtx]] – hSPIN1 + HBx <br />


*Spindlin-2B
*Spindlin-2B
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== References ==
== References ==
<references/>
<references/>
 
</StructureSection>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 10:42, 14 August 2024

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 29-May-2025

{{#tree:id=OrganizedByTopic|openlevels=0|

  • Spindlin-1
  • Spindlin-2B
    • 5lug – hSPIN2B + peptide
  • Spindlin-3
  • Spindlin-4
    • 4uy4 – hSPIN4 + histone peptide

}}

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. ↑ 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
  3. ↑ 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
  4. ↑ 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

Human spindlin-1 (skyblue) complex with histone H3 peptide (wheat) containing trimethyl lysine, MPD, Mg+2 (green) and Cl- (green) ions (PDB code 4mzg)

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Michal Harel, Joel L. Sussman, Alexander Berchansky
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