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Volume 584, Issue 3, Pages 477-481 (5 February 2010)


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On the role of the chaperonin CCT in the just-in-time assembly process of APC/CCdc20

Edited by Angel Nebreda

Carien DekkerCorresponding Author Informationemail address

Received 2 October 2009; received in revised form 16 November 2009; accepted 25 November 2009. published online 30 November 2009.

Abstract 

The just-in-time hypothesis relates to the assembly of large multi-protein complexes and their regulation of activation in the cell. Here I postulate that chaperonins may contribute to the timely assembly and activation of such complexes. For the case of anaphase promoting complex/cyclosomeCdc20 assembly by the eukaryotic chaperonin chaperonin containing Tcp1 it is shown that just-in-time synthesis and chaperone-assisted folding can synergise to generate a highly regulated assembly process of a protein complex that is vital for cell cycle progression. Once dependency has been established transcriptional regulation and chaperonin-dependency may have co-evolved to safeguard the timely activation of important multi-protein complexes.

Cell and Molecular Biology, The Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, United Kingdom

Corresponding Author InformationFax: +44 (0) 207 351 3325.

PII: S0014-5793(09)01028-X

doi:10.1016/j.febslet.2009.11.088


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