Interaction between TPX2 and ADD1 is important for the maintenance of spindle pole integrity.

• Main Authors: Wan-Yi Lin, 林宛儀
• Other Authors: Hong-Chen Chen
• Format: Others
• Language: zh-TW
• Published: 2016
• Online Access: http://ndltd.ncl.edu.tw/handle/45512278325732756251

碩士 === 國立中興大學 === 生物醫學研究所 === 104 === During mitosis, duplicated chromosomes are segregated by the mitotic spindle. Loss of spindle pole integrity leads to multipolar spindle formation and abnormal chromosomal segregation. TPX2, the targeting protein for Xenopus kinesin-like protein 2, is a microtubule-associated protein. TPX2 plays an important role in spindle pole organization and regulation of microtubule dynamics. Adducin-1（ADD1） is an actin-binding protein that has been shown to play important roles in the stabilization of the cortical cytoskeleton and cell–cell adhesions. Here, we found that TPX2 specifically interacts with Ser726 phosphorylated-ADD1 during M phase. Additionally, TPX2 is colocalized with Ser726 phosphorylated-ADD1 at mitotic centrosomes. We also show that the TPX2 depletion-induced multiple centrosomes results from centriole splitting in mitosis, which can be rescued by re-expression of HA tagged-TPX2 WT, but not of an TPX2 mutant defective in ADD1 binding. Taken together, our results suggest that the interaction between TPX2 and ADD1 at centrosomes is important for the maintenance of spindle pole integrity.