Researchers at the Center for Genomic Regulation (CRG) have discovered how proteins work in tandem to regulate 'treadmilling,' a mechanism used by the network of microtubules inside cells to ensure proper cell division. The findings are published in the Journal of Cell Biology.
Three proteins were found to be critical for regulating treadmilling: KIF2A, abelonging to a larger family of proteins that dismantles microtubules, the γ-tubulin ring complex , a scaffold for microtubules to grow from, and spastin, an enzyme that acts like a scissor cutting microtubules.
"The family of proteins that dismantle microtubules usually nibble on microtubules at both ends. We were surprised to find that one member of this family—KIF2A—has a strong preference for minus ends. This specialization is exactly what researchers have been looking for to explain why microtubules treadmill in the spindle," explains Dr. Thomas Surrey, senior author of the study and researcher at the Center for Genomic Regulation.
Before KIF2A can nibble a minus end, it needs to overcome yTuRC, which acts like a safety cap."The enzyme spastin is required to freefrom the safety cap so that KIF2A can do its job once microtubule plus ends have grown long enough," explains Dr. Cláudia Brito, co-first author of the study. The researchers found that the correct control of treadmilling requires the coordinated action of all three proteins. While the study does not directly translate into therapeutic avenues, it adds another piece to the intricate puzzle of cellular function and division.which must develop into many trillions of cells, all containing good copies of the genome.
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