Stathmin: Difference between revisions
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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 == | ||
'''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>. | '''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 == | ||