title: The condensin component NCAPG2 regulates microtubule-kinetochore attachment through recruitment of Polo-like kinase 1 to kinetochores.
abstract: The early event of microtubule-kinetochore attachment is a critical stage for precise chromosome segregation. Here we report that NCAPG2, which is a component of the condensin II complex, mediates chromosome segregation through microtubule-kinetochore attachment by recruiting PLK1 to prometaphase kinetochores. NCAPG2 colocalizes with PLK1 at prometaphase kinetochores and directly interacts with the polo-box domain (PBD) of PLK1 via its highly conserved C-terminal region. In both humans and Caenorhabditis elegans, when NCAPG2 is depleted, the attachment of the spindle to the kinetochore is loosened and misoriented. This is caused by the disruption of PLK1 localization to the kinetochore and by the decreased phosphorylation of its kinetochore substrate, BubR1. In addition, the crystal structure of the PBD of PLK1, in complex with the C-terminal region of NCAPG2, (1007)VLS-pT-L(1011), exhibits structural conservation of PBD-phosphopeptides, suggesting that the regulation of NCAPG2 function is phosphorylation-dependent. These findings suggest that NCAPG2 plays an important role in regulating proper chromosome segregation through a functional interaction with PLK1 during mitosis.
authors.affiliation: 1] Research Institute, National Cancer Center, Goyang, Gyeonggi 410-769, Republic of Korea [2].
authors.forename: Jae Hyeong
authors.initials: JH
authors.lastname: Kim
authors.affiliation: 1] Research Institute, National Cancer Center, Goyang, Gyeonggi 410-769, Republic of Korea [2].
authors.forename: Jaegal
authors.initials: J
authors.lastname: Shim
authors.affiliation: Research Institute, National Cancer Center, Goyang, Gyeonggi 410-769, Republic of Korea.
authors.forename: Min-Ju
authors.initials: MJ
authors.lastname: Ji
authors.affiliation: Research Institute, National Cancer Center, Goyang, Gyeonggi 410-769, Republic of Korea.
authors.forename: Yuna
authors.initials: Y
authors.lastname: Jung
authors.affiliation: Research Institute, National Cancer Center, Goyang, Gyeonggi 410-769, Republic of Korea.
authors.forename: Seoung Min
authors.initials: SM
authors.lastname: Bong
authors.affiliation: Laboratory of Cell Cycle and Signal Transduction, Department of Nanobiomedical Science and BK21 PLUS Research Center for Regenerative Medicine, Dankook University, Cheonan, Chungnam 330-714, Republic of Korea.
authors.forename: Young-Joo
authors.initials: YJ
authors.lastname: Jang
authors.affiliation: Research Institute, National Cancer Center, Goyang, Gyeonggi 410-769, Republic of Korea.
authors.forename: Eun-Kyung
authors.initials: EK
authors.lastname: Yoon
authors.affiliation: Research Institute, National Cancer Center, Goyang, Gyeonggi 410-769, Republic of Korea.
authors.forename: Sang-Jin
authors.initials: SJ
authors.lastname: Lee
authors.affiliation: Research Institute, National Cancer Center, Goyang, Gyeonggi 410-769, Republic of Korea.
authors.forename: Kwang Gi
authors.initials: KG
authors.lastname: Kim
authors.affiliation: Research Institute, National Cancer Center, Goyang, Gyeonggi 410-769, Republic of Korea.
authors.forename: Yon Hui
authors.initials: YH
authors.lastname: Kim
authors.affiliation: Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon, Gyeonggi 440-746, Republic of Korea.
authors.forename: Changwoo
authors.initials: C
authors.lastname: Lee
authors.affiliation: Research Institute, National Cancer Center, Goyang, Gyeonggi 410-769, Republic of Korea.
authors.forename: Byung Il
authors.initials: BI
authors.lastname: Lee
authors.affiliation: Research Institute, National Cancer Center, Goyang, Gyeonggi 410-769, Republic of Korea.
authors.forename: Kyung-Tae
authors.initials: KT
authors.lastname: Kim
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D020816:Amino Acid Motifs; D000818:Animals; D017173:Caenorhabditis elegans / Q000378:metabolism; D029742:Caenorhabditis elegans Proteins / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000378:metabolism*; D045744:Cell Line, Tumor; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D020090:Chromosome Segregation; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000378:metabolism; D005786:Gene Expression Regulation; D057809:HEK293 Cells; D006801:Humans; D018386:Kinetochores / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism*; D008938:Mitosis; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D010766:Phosphorylation; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011518:Proto-Oncogene Proteins / Q000378:metabolism*; D034622:RNA Interference; D000097869:Polo-Like Kinase 1
chemical_list: D000251:Adenosine Triphosphatases; D029742:Caenorhabditis elegans Proteins; D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D046912:Multiprotein Complexes; D017346:Protein Serine-Threonine Kinases; D011518:Proto-Oncogene Proteins; D000097869:Polo-Like Kinase 1; C000589016:NCAPG2 protein, human; C000599975:capg-2 protein, C elegans; C108312:condensin complexes; C584277:BUB1 protein, human