On the role of the chaperonin CCT in the just-in-time assembly process of APC/CCdc20.
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/cyclosome(Cdc20) 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.
Dekker
Carien
C
Cell and Molecular Biology, The Institute of Cancer Research, London, United Kingdom. cdekker@icr.ac.uk
D064173:Anaphase-Promoting Complex-Cyclosome; D000818:Animals; D056404:Chaperonin Containing TCP-1 / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D017510:Protein Folding; D043743:Ubiquitin-Protein Ligase Complexes / Q000378:metabolism*
D043743:Ubiquitin-Protein Ligase Complexes; D064173:Anaphase-Promoting Complex-Cyclosome; D056404:Chaperonin Containing TCP-1