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Published 10 April 2006. doi:10.1083/jcb.200510071
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 173, Number 1, 19-26
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 A dynamic ubiquitin equilibrium couples proteasomal activity to chromatin remodeling

Nico P. Dantuma1, Tom A.M. Groothuis2, Florian A. Salomons1, and Jacques Neefjes2

1 Department of Cell and Molecular Biology, The Medical Nobel Institute, Karolinska Institutet, S-171 77 Stockholm, Sweden
2 Division of Tumor Biology, The Netherlands Cancer Institute, 1066 CX, Amsterdam, Netherlands

Correspondence to Nico P. Dantuma: nico.dantuma{at}ki.se; or Jacques Neefjes: j.neefjes{at}nki.nl

Protein degradation, chromatin remodeling, and membrane trafficking are critically regulated by ubiquitylation. The presence of several coexisting ubiquitin-dependent processes, each of crucial importance to the cell, is remarkable. This brings up questions on how the usage of this versatile regulator is negotiated between the different cellular processes. During proteotoxic stress, the accumulation of ubiquitylated substrates coincides with the depletion of ubiquitylated histone H2A and chromatin remodeling. We show that this redistribution of ubiquitin during proteotoxic stress is a direct consequence of competition for the limited pool of free ubiquitin. Thus, the ubiquitin cycle couples various ubiquitin-dependent processes because of a rate-limiting pool of free ubiquitin. We propose that this ubiquitin equilibrium may allow cells to sense proteotoxic stress in a genome-wide fashion.

N.P. Dantuma and T.A.M. Groothius contributed equally to this paper.

Abbreviations used in this paper: GFP-Ub, GFP-ubiquitin; PAGFP, photoactivatable GFP; uH2A, ubiquitylated histone H2A.


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