| http://purl.uniprot.org/citations/34034836 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/34034836 | http://www.w3.org/2000/01/rdf-schema#comment | "Microtubule-severing protein (MTSP) is critical for the survival of both mitotic and postmitotic cells. However, the study of MTSP during meiosis of mammalian oocytes has not been reported. We found that spastin, a member of the MTSP family, was highly expressed in oocytes and aggregated in spindle microtubules. After knocking down spastin by specific siRNA, the spindle microtubule density of meiotic oocytes decreased significantly. When the oocytes were cultured in vitro, the oocytes lacking spastin showed an obvious maturation disorder. Considering the microtubule-severing activity of spastin, we speculate that spastin on spindles may increase the number of microtubule broken ends by severing the microtubules, therefore playing a nucleating role, promoting spindle assembly and ensuring normal meiosis. In addition, we found the colocalization and interaction of collapsin response mediator protein 5 (CRMP5) and spastin in oocytes. CRMP5 can provide structural support and promote microtubule aggregation, creating transportation routes, and can interact with spastin in the microtubule activity of nerve cells (30). Knocking down CRMP5 may lead to spindle abnormalities and developmental disorders in oocytes. Overexpression of spastin may reverse the abnormal phenotype caused by the deletion of CRMP5. In summary, our data support a model in which the interaction between spastin and CRMP5 promotes the assembly of spindle microtubules in oocytes by controlling microtubule dynamics, therefore ensuring normal meiosis."xsd:string |
| http://purl.uniprot.org/citations/34034836 | http://purl.org/dc/terms/identifier | "doi:10.1017/s0967199421000344"xsd:string |
| http://purl.uniprot.org/citations/34034836 | http://purl.uniprot.org/core/author | "Jin Z."xsd:string |
| http://purl.uniprot.org/citations/34034836 | http://purl.uniprot.org/core/author | "Shen Y."xsd:string |
| http://purl.uniprot.org/citations/34034836 | http://purl.uniprot.org/core/author | "Jiang S.S."xsd:string |
| http://purl.uniprot.org/citations/34034836 | http://purl.uniprot.org/core/author | "Liu J.W."xsd:string |
| http://purl.uniprot.org/citations/34034836 | http://purl.uniprot.org/core/author | "Gao L.L."xsd:string |
| http://purl.uniprot.org/citations/34034836 | http://purl.uniprot.org/core/author | "Cheng W.Y."xsd:string |
| http://purl.uniprot.org/citations/34034836 | http://purl.uniprot.org/core/author | "Shou H.F."xsd:string |
| http://purl.uniprot.org/citations/34034836 | http://purl.uniprot.org/core/date | "2022"xsd:gYear |
| http://purl.uniprot.org/citations/34034836 | http://purl.uniprot.org/core/name | "Zygote"xsd:string |
| http://purl.uniprot.org/citations/34034836 | http://purl.uniprot.org/core/pages | "80-91"xsd:string |
| http://purl.uniprot.org/citations/34034836 | http://purl.uniprot.org/core/title | "Spastin interacts with CRMP5 to promote spindle organization in mouse oocytes by severing microtubules."xsd:string |
| http://purl.uniprot.org/citations/34034836 | http://purl.uniprot.org/core/volume | "30"xsd:string |
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