A 60 kd cdc2-associated polypeptide complexes with the E1A proteins in adenovirus-infected cells

Giordano, A., Whyte, P., Harlow, E., Franza, B. R., Beach, D., Draetta, G. (September 1989) A 60 kd cdc2-associated polypeptide complexes with the E1A proteins in adenovirus-infected cells. Cell, 58 (5). pp. 981-90. ISSN 0092-8674

URL: http://www.ncbi.nlm.nih.gov/pubmed/2570639
DOI: 10.1016/0092-8674(89)90949-5


p60 is a cellular protein that binds to the adenovirus E1A protein complex in virally infected or transformed human cells. In both infected and uninfected cells, p60 was found in a complex with the cdc2 protein kinase. Immune complexes containing p60 and cdc2 display a cell cycle-dependent histone H1 kinase activity that is most active in interphase. The previously described cdc2-p62/cyclin complex also acts as a histone H1 kinase but is maximally active in mitotic metaphase. The shift in the timing of activation of different cdc2-containing complexes suggests that each might play a distinct role in regulation of the cell cycle.

Item Type: Paper
Uncontrolled Keywords: Adenovirus Early Proteins CDC2 Protein Kinase Cell Cycle DNA-Binding Proteins/*metabolism Electrophoresis, Gel, Two-Dimensional Hela Cells Humans Macromolecular Substances Molecular Weight Nuclear Proteins/*metabolism Oncogene Proteins, Viral/*metabolism Phosphoproteins/*metabolism Precipitin Tests Proliferating Cell Nuclear Antigen Protamine Kinase/metabolism Protein Binding Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.
Subjects: organism description > virus > adenovirus
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > cdc2
organs, tissues, organelles, cell types and functions > cell types and functions > cell functions > cell cycle
CSHL Authors:
Communities: CSHL labs > Beach lab
Depositing User: Gail Sherman
Date: 8 September 1989
Date Deposited: 18 Jul 2017 16:07
Last Modified: 18 Jul 2017 16:07
Related URLs:
URI: https://repository.cshl.edu/id/eprint/34853

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