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Titolo:
The centrosomal protein C-Nap1 is required for cell cycle-regulated centrosome cohesion
Autore:
Mayor, T; Stierhof, YD; Tanaka, K; Fry, AM; Nigg, EA;
Indirizzi:
Max Planck Inst Biochem, Dept Membrane Biochem, D-72076 Tubingen, Germany Max Planck Inst Biochem Tubingen Germany D-72076 72076 Tubingen, Germany Univ Geneva, Dept Biol Mol, CH-1211 Geneva, Switzerland Univ Geneva Geneva Switzerland CH-1211 Mol, CH-1211 Geneva, Switzerland
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 4, volume: 151, anno: 2000,
pagine: 837 - 846
SICI:
0021-9525(20001113)151:4<837:TCPCIR>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
SPINDLE FORMATION; KINASE; CENTRIOLE; ORGANIZATION; DUPLICATION; DYNAMICS; ANTIBODY; TUBULIN; CANCER; NEK2;
Keywords:
centrosome separation; mitotic spindle; centriole; C-Nap1; Nek2;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Nigg, EA Max Planck Inst Biochem, Dept Cell Biol, D-82152 Martinsried, Germany Max Planck Inst Biochem Martinsried Germany D-82152 ed, Germany
Citazione:
T. Mayor et al., "The centrosomal protein C-Nap1 is required for cell cycle-regulated centrosome cohesion", J CELL BIOL, 151(4), 2000, pp. 837-846

Abstract

Duplicating centrosomes are paired during interphase, but are separated atthe onset of mitosis, Although the mechanisms controlling centrosome cohesion and separation are important for centrosome function throughout the cell cycle, they remain poorly understood. Recently, we have proposed that C-Nap1, a novel centrosomal protein, is part of a structure linking parental centrioles in a cell cycle-regulated manner. To test this model, we have performed a detailed structure-function analysis on C-Nap1. We demonstrate that antibody-mediated interference with C-Nap1 function causes centrosome splitting, regardless of the cell cycle phase. Splitting occurs between parental centrioles and is not dependent on the presence of an intact microtubuleor microfilament network. Centrosome splitting can also be induced by overexpression of truncated C-Nap1 mutants, but not full-length protein. Antibodies raised against different domains of C-Nap1 prove that this protein dissociates from spindle poles during mitosis, but reaccumulates at centrosomes at the end of cell division. Use of the same antibodies in immuno-electron microscopy shows that C-Nap1 is confined to the proximal end domains of centrioles, indicating that a putative linker structure must contain additional proteins. We conclude that C-Nap1 is a key component of a dynamic, cellcycle-regulated structure that mediates centriole-centriole cohesion.

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Documento generato il 05/12/20 alle ore 19:51:49