Published online 5 March 2001. doi:10.1083/jcb.152.5.945
© The Rockefeller University Press,
0021-9525/2001//945 $5.00
The Journal of Cell Biology, Volume 152, Number 5,
, 2001 945-958
The Localization of Human Cyclins B1 and B2 Determines Cdk1 Substrate Specificity and Neither Enzyme Requires Mek to Disassemble the Golgi Apparatus
Viji Mythily Draviama,
Simona Orrechiab,
Martin Lowec,
Ruggero Pardib, and
Jonathon Pinesa
a Wellcome/Cancer Research Campaign Institute and Department of Zoology, Cambridge CB2 1QR, United Kingdom
b Vita Salute University School of Medicine, Scientific Institute San Raffaele, Milan I-20132, Italy
c Division of Biochemistry, School of Biological Sciences, University of Manchester, Manchester M13 9PT, United Kingdom
Wellcome/CRC Institute, Department of Zoology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QR, UK.44-1223-33-408944-1223-33-4096
jp103{at}mole.bio.cam.ac.uk
In this paper, we show that substrate specificity is primarily conferred on human mitotic cyclin-dependent kinases (CDKs) by their subcellular localization. The difference in localization of the B-type cyclin–CDKs underlies the ability of cyclin B1–CDK1 to cause chromosome condensation, reorganization of the microtubules, and disassembly of the nuclear lamina and of the Golgi apparatus, while it restricts cyclin B2–CDK1 to disassembly of the Golgi apparatus. We identify the region of cyclin B2 responsible for its localization and show that this will direct cyclin B1 to the Golgi apparatus and confer upon it the more limited properties of cyclin B2. Equally, directing cyclin B2 to the cytoplasm with the NH2 terminus of cyclin B1 confers the broader properties of cyclin B1. Furthermore, we show that the disassembly of the Golgi apparatus initiated by either mitotic cyclin–CDK complex does not require mitogen-activated protein kinase kinase (MEK) activity.
Key Words: cyclin CDK mitosis protein kinase Golgi apparatus
© 2001 The Rockefeller University Press
Abbreviations used in this paper: CDK, cyclin-dependent kinase; ERK, extracellular singal–regulated kinase; GFP, green fluorescent protein; LMB, leptomycin B; MAP, mitogen-activated protein; MEK, MAP kinase kinase; NAGT, N-acetyglucosaminyltransferase 1.

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