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© The Rockefeller University Press, 0021-9525/1999//791 $5.00
The Journal of Cell Biology, Volume 146, Number 4, , 1999 791-800

Original Article

Regulation of APC Activity by Phosphorylation and Regulatory Factors



Shuji Kotania, Hirofumi Tanakab, Hideyo Yasudab, and Kazuo Todokoroa

a Tsukuba Life Science Center, The Institute of Physical and Chemical Research, Tsukuba, Ibaraki 305-0074, Japan
b School of Life Science, Tokyo University of Pharmacy and Life Science, Hachiooji, Tokyo 192-0355, Japan
Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN), 3-1, Koyadai, Tsukuba, Ibaraki 305-0074, Japan.81-298-36-909081-298-36-9075

todokoro{at}rtc.riken.go.jp

Ubiquitin-dependent proteolysis of Cut2/Pds1 and Cyclin B is required for sister chromatid separation and exit from mitosis, respectively. Anaphase-promoting complex/cyclosome (APC) specifically ubiquitinates Cut2/Pds1 at metaphase–anaphase transition, and ubiquitinates Cyclin B in late mitosis and G1 phase. However, the exact regulatory mechanism of substrate-specific activation of mammalian APC with the right timing remains to be elucidated. We found that not only the binding of the activators Cdc20 and Cdh1 and the inhibitor Mad2 to APC, but also the phosphorylation of Cdc20 and Cdh1 by Cdc2-Cyclin B and that of APC by Polo-like kinase and cAMP-dependent protein kinase, regulate APC activity. The cooperation of the phosphorylation/dephosphorylation and the regulatory factors in regulation of APC activity may thus control the precise progression of mitosis.

Key Words: anaphase-promoting complex • Cdc20 • Cdh1 • Mad2 • phosphorylation

© 1999 The Rockefeller University Press

1.used in this paper: APC, anaphase promoting complex/cyclosome; MPF, Cdc2-Cyclin B or Cdc2-GST-Cyclin B; pAPC, APC phosphorylated by pPlk or APlk-activated APC; pCdc20, Cdc20 phosphorylated by MPF; pCdh1, Cdh1 phosphorylated MPF; PKA, cAMP-dependent protein kinase; Plk, Polo-like kinase; pPlk, Plk phosphorylated by MPF


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