CRMP5 participates in oocyte meiosis by regulating spastin to correct microtubule-kinetochore misconnection
Our previous studies have suggested that spastin, which aggregates on spindle microtubules in oocytes, may promote the assembly of mouse oocyte spindles by cutting microtubules. This action may be related to CRMP5, as knocking down CRMP5 results in reduced spindle microtubule density and maturation...
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| Veröffentlicht in: | Zygote (Cambridge) 2024-02, Vol.32 (1), p.21-27 |
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| creator | Jin, Zhen Zhang, Zhi-Cai Xiao, Chen-Yu Li, Mei-Qi Li, Qian-Ru Gao, Lei-Lei |
| description | Our previous studies have suggested that spastin, which aggregates on spindle microtubules in oocytes, may promote the assembly of mouse oocyte spindles by cutting microtubules. This action may be related to CRMP5, as knocking down CRMP5 results in reduced spindle microtubule density and maturation defects in oocytes. In this study, we found that, after knocking down CRMP5 in oocytes, spastin distribution shifted from the spindle to the spindle poles and errors in microtubule-kinetochore attachment appeared in oocyte spindles. However, CRMP5 did not interact with the other two microtubule-severing proteins, katanin-like-1 (KATNAL1) and fidgetin-like-1 (FIGNL1), which aggregate at the spindle poles. We speculate that, in oocytes, due to the reduction of spastin distribution on chromosomes after knocking down CRMP5, microtubule-kinetochore errors cannot be corrected through severing, resulting in meiotic division abnormalities and maturation defects in oocytes. This finding provides new insights into the regulatory mechanisms of spastin in oocytes and important opportunities for the study of meiotic division mechanisms. |
| doi_str_mv | 10.1017/S0967199423000564 |
| format | Article |
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This action may be related to CRMP5, as knocking down CRMP5 results in reduced spindle microtubule density and maturation defects in oocytes. In this study, we found that, after knocking down CRMP5 in oocytes, spastin distribution shifted from the spindle to the spindle poles and errors in microtubule-kinetochore attachment appeared in oocyte spindles. However, CRMP5 did not interact with the other two microtubule-severing proteins, katanin-like-1 (KATNAL1) and fidgetin-like-1 (FIGNL1), which aggregate at the spindle poles. We speculate that, in oocytes, due to the reduction of spastin distribution on chromosomes after knocking down CRMP5, microtubule-kinetochore errors cannot be corrected through severing, resulting in meiotic division abnormalities and maturation defects in oocytes. This finding provides new insights into the regulatory mechanisms of spastin in oocytes and important opportunities for the study of meiotic division mechanisms.</description><identifier>ISSN: 0967-1994</identifier><identifier>EISSN: 1469-8730</identifier><identifier>DOI: 10.1017/S0967199423000564</identifier><identifier>PMID: 38047349</identifier><language>eng</language><publisher>England: Cambridge University Press</publisher><subject>Abnormalities ; Animals ; Antibodies ; Cell division ; Chromosomes ; Defects ; Errors ; Gametocytes ; In vitro fertilization ; Kinetochores - metabolism ; Maturation ; Meiosis ; Mice ; Microtubules ; Microtubules - metabolism ; Oocytes ; Oocytes - physiology ; Ovaries ; Poles ; Polymerization ; Proteins ; Regulatory mechanisms (biology) ; RNA polymerase ; Spastin - genetics ; Spastin - metabolism ; Spindle Apparatus - physiology ; Spindles</subject><ispartof>Zygote (Cambridge), 2024-02, Vol.32 (1), p.21-27</ispartof><rights>The Author(s), 2023. 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| subjects | Abnormalities Animals Antibodies Cell division Chromosomes Defects Errors Gametocytes In vitro fertilization Kinetochores - metabolism Maturation Meiosis Mice Microtubules Microtubules - metabolism Oocytes Oocytes - physiology Ovaries Poles Polymerization Proteins Regulatory mechanisms (biology) RNA polymerase Spastin - genetics Spastin - metabolism Spindle Apparatus - physiology Spindles |
| title | CRMP5 participates in oocyte meiosis by regulating spastin to correct microtubule-kinetochore misconnection |
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