Plk1-dependent and -independent roles of an ODF2 splice variant, hCenexin1, at the centrosome of somatic cells.
Outer dense fiber 2 (ODF2) was initially identified as a major component of the sperm tail cytoskeleton, and was later suggested to be localized to somatic centrosomes and required for the formation of primary cilia. Here we show that a splice variant of hODF2 called hCenexin1, but not hODF2 itself, efficiently localizes to somatic centrosomes via a variant-specific C-terminal extension and recruits Plk1 through a Cdc2-dependent phospho-S796 motif within the extension. This interaction and Plk1 activity were important for proper recruitment of pericentrin and gamma-tubulin, and, ultimately, for formation of normal bipolar spindles. Earlier in the cell cycle, hCenexin1, but again not hODF2, also contributed to centrosomal recruitment of ninein and primary cilia formation independent of Plk1 interaction. These findings provide a striking example of how a splice-generated C-terminal extension of a sperm tail-associating protein mediates unanticipated centrosomal events at distinct stages of the somatic cell cycle.
Soung
Nak-Kyun
NK
Laboratory of Metabolism, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Park
Jung-Eun
JE
Yu
Li-Rong
LR
Lee
Kyung H
KH
Lee
Jung-Min
JM
Bang
Jeong K
JK
Veenstra
Timothy D
TD
Rhee
Kunsoo
K
Lee
Kyung S
KS
D017398:Alternative Splicing / Q000235:genetics*; D000595:Amino Acid Sequence; D000941:Antigens / Q000378:metabolism; D016203:CDC2 Protein Kinase / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000378:metabolism*; D018385:Centrosome / Q000201:enzymology*; D002923:Cilia / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000378:metabolism; D006367:HeLa Cells; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D022101:Microtubule-Organizing Center / Q000201:enzymology; D008938:Mitosis; D008954:Models, Biological; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000378:metabolism; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D011518:Proto-Oncogene Proteins / Q000378:metabolism*; D014404:Tubulin / Q000378:metabolism; D000097869:Polo-Like Kinase 1
D000941:Antigens; D016203:CDC2 Protein Kinase; D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins; D006360:Heat-Shock Proteins; D009687:Nuclear Proteins; D010768:Phosphoserine; D017346:Protein Serine-Threonine Kinases; D011518:Proto-Oncogene Proteins; D014404:Tubulin; D000097869:Polo-Like Kinase 1; C512806:NIN protein, human; C490107:ODF2 protein, human; C086178:pericentrin