title: Centromere Protein (CENP)-W Interacts with Heterogeneous Nuclear Ribonucleoprotein (hnRNP) U and May Contribute to Kinetochore-Microtubule Attachment in Mitotic Cells.
abstract: BACKGROUND
  Recent studies have shown that heterogeneous nuclear ribonucleoprotein U (hnRNP U), a component of the hnRNP complex, contributes to stabilize the kinetochore-microtubule interaction during mitosis. CENP-W was identified as an inner centromere component that plays crucial roles in the formation of a functional kinetochore complex.
  
  
  RESULTS
  We report that hnRNP U interacts with CENP-W, and the interaction between hnRNP U and CENP-W mutually increased each other's protein stability by inhibiting the proteasome-mediated degradation. Further, their co-localization was observed chiefly in the nuclear matrix region and at the microtubule-kinetochore interface during interphase and mitosis, respectively. Both microtubule-stabilizing and microtubule-destabilizing agents significantly decreased the protein stability of CENP-W. Furthermore, loss of microtubules and defects in microtubule organization were observed in CENP-W-depleted cells.
  
  
  CONCLUSIONS
  Our data imply that CENP-W plays an important role in the attachment and interaction between microtubules and kinetochore during mitosis.
authors.affiliation: Department of Microbiology and Molecular Biology, College of Bioscience and Biotechnology, Chungnam National University, Daejeon, Republic of Korea.
authors.forename: Younghwa
authors.initials: Y
authors.lastname: Chun
authors.affiliation: Department of Microbiology and Molecular Biology, College of Bioscience and Biotechnology, Chungnam National University, Daejeon, Republic of Korea.
authors.forename: Raehyung
authors.initials: R
authors.lastname: Kim
authors.affiliation: Department of Microbiology and Molecular Biology, College of Bioscience and Biotechnology, Chungnam National University, Daejeon, Republic of Korea.
authors.forename: Soojin
authors.initials: S
authors.lastname: Lee
mesh_terms: D001665:Binding Sites; D002868:Chromosomal Proteins, Non-Histone / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D005786:Gene Expression Regulation; D057809:HEK293 Cells; D006367:HeLa Cells; D034441:Heterogeneous-Nuclear Ribonucleoproteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D018386:Kinetochores / Q000378:metabolism / Q000502:physiology* / Q000648:ultrastructure; D008856:Microscopy, Fluorescence; D008870:Microtubules / Q000378:metabolism / Q000502:physiology* / Q000648:ultrastructure; D008938:Mitosis; D015530:Nuclear Matrix / Q000378:metabolism / Q000648:ultrastructure; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D011485:Protein Binding; D055550:Protein Stability; D059748:Proteolysis; D034741:RNA, Small Interfering / Q000235:genetics / Q000378:metabolism; D015398:Signal Transduction; D008941:Spindle Apparatus / Q000378:metabolism / Q000502:physiology / Q000648:ultrastructure
chemical_list: C534000:CENPW protein, human; D002868:Chromosomal Proteins, Non-Histone; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D034741:RNA, Small Interfering; D046988:Proteasome Endopeptidase Complex