Calcium-dependent regulator protein: localization in mitotic apparatus of eukaryotic cells.
Calcium-dependent regulator protein is a low molecular weight (17,000), thermostable, calcium binding protein which is structurally homologous to skeletal muscle troponin C. This protein is present in all nonmuscle cells and has been shown to decorate stress fibers in interphase cells by indirect immunofluorescence. Using this procedure we have investigated the distribution of the protein during mitosis of eukaryotic cells. As the cells enter prophase, the distinct cytoplasmic localization disappears commensurate with the dissolution of the cytoskeleton. The regulator protein seems to be randomly distributed throughout the prophase cell, including the region around the condensed chromosomes. However, at prometaphase, it is localized in association with the half-spindles of the mitotic apparatus. Through metaphase and most of anaphase, the protein remains localized between the chromosomes and the poles of the spindle. During late anaphase the protein is also found in the interzone region but rapidly condenses into two small regions, one on each side of the midbody that separates the daughter cells. The regulator protein is not localized in the cleavage furrow during telophase, whereas actin is demonstrable in this region. Indeed, placement of the protein during mitosis is distinct from both that of actin and that of tubulin. The localization of calcium-dependent regulator protein during mitosis suggests that it may mediate the calcium effects on the mitotic apparatus and thus play a role in chromosome movement.
D000199:Actins / Q000378:metabolism; D000705:Anaphase; D002118:Calcium / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D002460:Cell Line; D007399:Interphase; D008677:Metaphase; D008870:Microtubules / Q000378:metabolism; D008938:Mitosis; D009940:Organoids / Q000378:metabolism*; D011418:Prophase; D013692:Telophase
D000199:Actins; D002352:Carrier Proteins; D002118:Calcium
J Cell Biol. 1977 Sep;74(3):794-815
71303
J Cell Biol. 1976 Dec;71(3):848-75
62755
J Biol Chem. 1978 Jan 25;253(2):343-6
201628
J Biol Chem. 1977 Dec 10;252(23):8415-22
200611
J Biol Chem. 1977 Apr 10;252(7):2437-40
191460
Proc Natl Acad Sci U S A. 1977 Apr;74(4):1610-3
140377
Biochem Biophys Res Commun. 1977 Oct 24;78(4):1263-72
144501
J Cell Biol. 1977 Mar;72(3):552-67
320217
J Cell Biol. 1975 Dec;67(3):789-800
1238405
J Biol Chem. 1971 May 10;246(9):2859-69
4324340
Biochim Biophys Acta. 1974 Apr 25;341(2):402-11
4365089
J Biol Chem. 1973 Sep 10;248(17):5950-5
4353626
Biochem Biophys Res Commun. 1970 Feb 6;38(3):533-8
4315350
Exp Cell Res. 1973 Sep;81(1):87-94
4271272
Exp Cell Res. 1972 Feb;70(2):325-32
4258131
Proc Natl Acad Sci U S A. 1974 Jun;71(6):2268-72
4210210
Proc Natl Acad Sci U S A. 1973 Jun;70(6):1688-92
4578441
Exp Cell Res. 1974 May;86(1):161-4
4598461
J Biol Chem. 1976 Aug 10;251(15):4495-500
181374
Adv Cyclic Nucleotide Res. 1975;5:179-94
165665
Biochem J. 1975 Jan;146(1):109-20
167710
Biochem Biophys Res Commun. 1975 Aug 4;65(3):975-82
168896
Proc Natl Acad Sci U S A. 1975 Dec;72(12):4981-5
174086
Science. 1975 Mar 14;187(4180):948-50
1096300
Proc Natl Acad Sci U S A. 1975 Jun;72(6):2451-5
1094471
Exp Cell Res. 1975 Sep;94(2):409-25
1238267
J Cell Biol. 1975 Dec;67(3):501-17
1238403