TY - JOUR
T1 - Phosphorylation of Centrin during the Cell Cycle and Its Role in Centriole Separation Preceding Centrosome Duplication
AU - Lutz, Ward
AU - Lingle, Wilma L.
AU - McCormick, Daniel
AU - Greenwood, Tammy M.
AU - Salisbury, Jeffrey L.
PY - 2001/6/8
Y1 - 2001/6/8
N2 - Once during each cell cycle, mitotic spindle poles arise by separation of newly duplicated centrosomes. We report here the involvement of phosphorylation of the centrosomal protein centrin in this process. We show that centrin is phosphorylated at serine residue 170 during the G2/M phase of the cell cycle. Indirect immunofluorescence staining of HeLa cells using a phosphocentrin-specific antibody reveals intense labeling of mitotic spindle poles during prophase and metaphase of the cell division cycle, with diminished staining of anaphase and no staining of telophase and interphase centrosomes. Cultured cells undergo a dramatic increase in centrin phosphorylation following the experimental elevation of PKA activity, suggesting that this kinase can phosphorylate centrin in vivo. Surprisingly, elevated PKA activity also resulted intense phosphocentrin antibody labeling of interphase centrosomes and in the concurrent movement of individual centrioles apart from one another. Taken together, these results suggest that centrin phosphorylation signals the separation of centrosomes at prophase and implicates centrin phosphorylation in centriole separation that normally precedes centrosome duplication.
AB - Once during each cell cycle, mitotic spindle poles arise by separation of newly duplicated centrosomes. We report here the involvement of phosphorylation of the centrosomal protein centrin in this process. We show that centrin is phosphorylated at serine residue 170 during the G2/M phase of the cell cycle. Indirect immunofluorescence staining of HeLa cells using a phosphocentrin-specific antibody reveals intense labeling of mitotic spindle poles during prophase and metaphase of the cell division cycle, with diminished staining of anaphase and no staining of telophase and interphase centrosomes. Cultured cells undergo a dramatic increase in centrin phosphorylation following the experimental elevation of PKA activity, suggesting that this kinase can phosphorylate centrin in vivo. Surprisingly, elevated PKA activity also resulted intense phosphocentrin antibody labeling of interphase centrosomes and in the concurrent movement of individual centrioles apart from one another. Taken together, these results suggest that centrin phosphorylation signals the separation of centrosomes at prophase and implicates centrin phosphorylation in centriole separation that normally precedes centrosome duplication.
UR - http://www.scopus.com/inward/record.url?scp=0035827607&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035827607&partnerID=8YFLogxK
U2 - 10.1074/jbc.M101324200
DO - 10.1074/jbc.M101324200
M3 - Article
C2 - 11279195
AN - SCOPUS:0035827607
SN - 0021-9258
VL - 276
SP - 20774
EP - 20780
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 23
ER -