【摘 要】
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Microtubules (MTs) are regulated by a number of known posttranslational modifications (PTMs) on α/β-tubulin to fulfill diverse cellular functions.Here,we show
【机 构】
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State Key Laboratory of Cell Biology,CAS Center for Excellence in Molecular Cell Science/Shanghai In
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Microtubules (MTs) are regulated by a number of known posttranslational modifications (PTMs) on α/β-tubulin to fulfill diverse cellular functions.Here,we showed that SUMOylation is a novel PTM on α-tubulin in vivo and in vitro.The SUMOylation on α-tubulin mainly occurred at Lys 96 (K96),K166,and 1304 of soluble α-tubulin and could be removed by small ubiquitin-related modifier (SUMO)-specific peptidase 1.In vitro experiments showed that tubulin SUMOylation could reduce interprotofilament interaction,promote MT catastrophe,and impede MT polymerization.In cells,mutation of the SUMOylation sites on α-tubulin reduced catastrophe frequency and increased the proportion of polymerized α-tubulin,while upregulation of SUMOylation with fusion of SUM01 reduced α-tubulin assembly into MTs.Additionally,overexpression of SUMOylation-deficient α-tubulin attenuated the neurite extension in Neuro-2a cells.Thus,SUMOylation on α-tubulin represents a new player in the regulation of MT properties.
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