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Stathmin

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<StructureSection load='3ryf' size='340' side='right' caption='Rat stathmin SLD domain (magenta) complex with tubulin α chain (grey, pink), tubulin β chain (green, yellow), GTP, sulfate and Mg+2 ions (PDB code [[3ryf]])' scene=''>
<StructureSection load='3ryf' size='340' side='right' caption='Rat stathmin SLD domain (magenta) complex with tubulin α chain (grey, pink), tubulin β chain (green, yellow), GTP, sulfate and Mg+2 ions (PDB code [[3ryf]])' scene=''>
== Function ==
== Function ==
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'''Stathmin-4''' (STM-4) regulates microtubules dynamics. Microtubules undergo continuous assembly and disassembly in the cell’s cytoskeleton. STM-4 binds to tubulin and prevents the latter from polymerization thus preventing microtubule assembly. Phosphorylation of STM-4 weakens the binding of STM-4 to tubulin enabling the microtubule assembly needed for the formation of mitotic spindle. Thus, STM-4 is an oncoprotein. STM-4 contains an SLD (Stathmin-Like Domain) domain of 149 residues which binds the tubulin dimer<ref>PMID:15216892</ref>.
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'''Stathmin-4''' (STM-4) or '''stathmin-like protein B3''' regulates microtubules dynamics. Microtubules undergo continuous assembly and disassembly in the cell’s cytoskeleton. STM-4 binds to tubulin and prevents the latter from polymerization thus preventing microtubule assembly. Phosphorylation of STM-4 weakens the binding of STM-4 to tubulin enabling the microtubule assembly needed for the formation of mitotic spindle. Thus, STM-4 is an oncoprotein. STM-4 contains an SLD (Stathmin-Like Domain) domain of 149 residues which binds the tubulin dimer<ref>PMID:15216892</ref>.
== Disease ==
== Disease ==
Decreased levels of STM-4 are found in brains of adults with Down syndrome and Alzheimer disease<ref>PMID:11771751</ref>.
Decreased levels of STM-4 are found in brains of adults with Down syndrome and Alzheimer disease<ref>PMID:11771751</ref>.
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</StructureSection>
 
== 3D Structures of stathmin-4 ==
== 3D Structures of stathmin-4 ==
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[[Stathmin-4 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Stathmin SLD domain complex with tubulin
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**[[3ryf]] – rSTM + tubulin + GTP - rat<br />
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**[[3hkb]], [[3ryc]], [[3ryi]] – rSTM + tubulin + GTP + GDP <br />
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**[[3ryh]] – rSTM + tubulin + GTP + phosphomethylphosphonic acid guanylate <br />
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**[[3hkc]], [[3n2g]], [[3n2k]] – rSTM + tubulin + GTP + GDP + pyridine derivative <br />
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**[[3hkd]] – rSTM + tubulin + GTP + GDP + pyrrolidine derivative <br />
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**[[3hke]] – rSTM + tubulin + GTP + GDP + benzenesulfonamide derivative <br />
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*Stathmin SLD domain complex with tubulin and drugs
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**[[1sa0]] – rSTM + tubulin + GTP + GDP + anti-gout drug <br />
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**[[1sa1]], [[1z2b]] – rSTM + tubulin + GTP + GDP + anti-wart drug <br />
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**[[4eb6]], [[5j2u]] – rSTM (mutant) + tubulin + GTP + GDP + anti-cancer drug <br />
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**[[3du7]] – rSTM + tubulin + GTP + GDP + phomopsine + anti-gout drug <br />
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**[[3e22]] – rSTM + tubulin + GTP + GDP + soblidotine + anti-gout drug <br />
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**[[5lp6]], [[5kx5]] – rSTM + tubulin + GTP + GDP + drug <br />
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**[[3ut5]] – rSTM (mutant) + tubulin + GTP + GDP + ustiloxine + anti-gout drug + Vinca tetrapeptide<br />
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*Stathmin SLD domain complex with tubulin and tubulin tyrosine ligase
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**[[4iij]] – rSTM + tubulin + tubulin tyrosine ligase + GTP + GDP <br />
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**[[4ihj]] – rSTM + tubulin + tubulin tyrosine ligase + GTP + GDP + ADP <br />
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**[[5jqg]], [[6i5c]], [[4i55]], [[5xp3]] – rSTM-4 + tubulin + tubulin tyrosine ligase + GTP + GDP + ATP derivative <br />
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**[[5yl2]], [[5ylj]], [[5yls]], [[6br1]], [[6brf]], [[6bry]], [[6bs2]], [[6d88]], [[6fkj]], [[6fkl]], [[5o7a]] – rSTM-4 + tubulin + tubulin tyrosine ligase + GTP + GDP + ATP derivative + inhibitor <br />
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**[[5xkf]] – rSTM-4 + tubulin + tubulin tyrosine ligase + GTP + GDP + inhibitor<br />
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**[[4o2a]] – rSTM + tubulin + tubulin tyrosine ligase + GTP + GDP + ADP + inhibitor<br />
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**[[5lov]], [[5njh]] – rSTM + tubulin + tubulin tyrosine ligase + GTP + GDP + ATP derivative + azoamide<br />
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**[[5lxs]], [[5lxt]] – rSTM + tubulin + tubulin tyrosine ligase + GTP + GDP + ATP derivative + discodermolide<br />
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**[[5lyj]], [[5mf4]] – rSTM + tubulin + tubulin tyrosine ligase + GTP + GDP + ATP derivative + natural product<br />
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*Stathmin SLD domain complex with tubulin, tubulin tyrosine ligase and drug
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**[[5xiw]] – rSTM-4 + tubulin + tubulin tyrosine ligase + GTP + GDP + anti-gout drug <br />
 
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**[[5xke]] – rSTM-4 + tubulin + protein + GTP + GDP + anti-gout drug<br />
 
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**[[4o2b]] – rSTM + tubulin + tubulin tyrosine ligase + GTP + GDP + ATP derivative + anti-gout drug<br />
 
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**[[5xkh]] – rSTM-4 + tubulin + protein + GTP + GDP + anti-cancer drug<br />
 
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**[[4o4l]], [[5j2t]], [[5bmv]], [[5la6]], [[5jh7]], [[5jvd]], [[5fnv]], [[5c8y]], [[5ca0]], [[5ca1]], [[5cb4]], [[4yj2]], [[4yj3]], [[4x1i]], [[4x1k]], [[4x1y]], [[4x20]], [[4tuy]], [[4zol]], [[4tv8]], [[4tv9]], [[4o4j]], [[4o4l]], [[5i50]], [[4i4t]], [[4o4i]], [[4o2l]], [[5iyz]], [[5la6]], [[5m7e]], [[5m7g]], [[5m8d]], [[5m8g]], [[5xlt]], [[5yl4]], [[5xkg]], [[5xlt]], [[6fii]], [[6fjf]], [[6fjm]], [[5xlz]], [[4i50]] – rSTM-4 + tubulin + tubulin tyrosine ligase + GTP + GDP + ATP derivative + anti-cancer drugs<br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Rat stathmin SLD domain (magenta) complex with tubulin α chain (grey, pink), tubulin β chain (green, yellow), GTP, sulfate and Mg+2 ions (PDB code 3ryf)

Drag the structure with the mouse to rotate

References

  1. ↑ Curmi PA, Gavet O, Charbaut E, Ozon S, Lachkar-Colmerauer S, Manceau V, Siavoshian S, Maucuer A, Sobel A. Stathmin and its phosphoprotein family: general properties, biochemical and functional interaction with tubulin. Cell Struct Funct. 1999 Oct;24(5):345-57. PMID:15216892
  2. ↑ Cheon MS, Fountoulakis M, Cairns NJ, Dierssen M, Herkner K, Lubec G. Decreased protein levels of stathmin in adult brains with Down syndrome and Alzheimer's disease. J Neural Transm Suppl. 2001;(61):281-8. PMID:11771751

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Joel L. Sussman

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