@article{e7ede45911064ac0a96669bc0fb5c080,
title = "Septin 7 is a centrosomal protein that ensures S phase entry and microtubule nucleation by maintaining the abundance of p150glued",
abstract = "Septins play important roles in regulating development and differentiation. Septin 7 (SEPT7) is a crucial component in orchestrating the septin core complex into highly ordered filamentous structures. Here, we showed that genetic depletion of SEPT7 or treatment with forchlorfenuron (FCF; a compound known to affect septin filament assembly) led to reduced the S phase entry in cell models and zebrafish embryos. In addition to colocalizing with actin filaments, SEPT7 resided in the centrosome, and SEPT7 depletion led to aberrant mitotic spindle pole formation. This mitotic defect was rescued in SEPT7-deficient cells by wild-type SEPT7, suggesting that SEPT7 maintained mitotic spindle poles. In addition, we observed disorganized microtubule nucleation and reduced cell migration with SEPT7 depletion. Furthermore, SEPT7 formed a complex with and maintained the abundance of p150glued, the component of centriole subdistal appendages. Depletion of p150glued resulted in a phenotype reminiscent of SEPT7-deficient cells, and overexpression of p150glued reversed the defective phenotypes. Thus, SEPT7 is a centrosomal protein that maintains proper cell proliferation and microtubule array formation via maintaining the abundance of p150glued.",
author = "Chen, {Ting Yu} and Lin, {Tzu Chien} and Kuo, {Pao Lin} and Chen, {Zi Rong} and Cheng, {Hui ling} and Chao, {Yu Ying} and Syu, {Jhih Siang} and Lu, {Fu I.} and Wang, {Chia Yih}",
note = "Funding Information: This study was supported by grants from the Ministry of Science and Technology (MOST106-2320-B-006-056-MY3, MOST109-2320-B-006-042-MY3, and MOST 109-2320-B-006 -034) to Chia-Yih Wang; (MOST 104-2311-B-006 -005 -MY3 and MOST 107-2311-B-006-001) to Fu-I Lu. This study was supported in part by the Ministry of Education, Taiwan, ROC, The Aim for the Top University Project to National Cheng Kung University (NCKU). This study received funding from the Headquarters of University Advancement at National Cheng Kung University, which is sponsored by the Ministry of Education, Taiwan, ROC. This study was supported in part by (received funding from) the Headquarters of University Advancement at National Cheng Kung University, which is sponsored by the Ministry of Education, Taiwan, ROC. This work was in part financially supported by the iEGG and Animal Biotechnology Center from The Feature Area Research Center Program within the framework of the Higher Education Sprout Project by the Ministry of Education (MOE) in Taiwan (MOE-107-S-0023-F). Funding Information: This study was supported by grants from the Ministry of Science and Technology (MOST106‐2320‐B‐006‐056‐MY3, MOST109‐2320‐B‐006‐042‐MY3, and MOST 109‐2320‐B‐006 ‐034) to Chia‐Yih Wang; (MOST 104‐2311‐B‐006 ‐005 ‐MY3 and MOST 107‐2311‐B‐006‐001) to Fu‐I Lu. This study was supported in part by the Ministry of Education, Taiwan, ROC, The Aim for the Top University Project to National Cheng Kung University (NCKU). This study received funding from the Headquarters of University Advancement at National Cheng Kung University, which is sponsored by the Ministry of Education, Taiwan, ROC. This study was supported in part by (received funding from) the Headquarters of University Advancement at National Cheng Kung University, which is sponsored by the Ministry of Education, Taiwan, ROC. This work was in part financially supported by the iEGG and Animal Biotechnology Center from The Feature Area Research Center Program within the framework of the Higher Education Sprout Project by the Ministry of Education (MOE) in Taiwan (MOE‐107‐S‐0023‐F). Publisher Copyright: {\textcopyright} 2020 Wiley Periodicals LLC",
year = "2021",
month = apr,
doi = "10.1002/jcp.30037",
language = "English",
volume = "236",
pages = "2706--2724",
journal = "Journal of Cellular Physiology",
issn = "0021-9541",
publisher = "Wiley-Liss Inc.",
number = "4",
}