Not-so-pseudo a substrate: Acm1-mediated inhibition of the APC.
In a recent issue of Molecular Cell, Enquist-Newman et al. (2008) demonstrate that Acm1 is ubiquitinated by APC(Cdc20). By contrast, the high-affinity interaction between Acm1 and APC(Cdh1) renders it a poor substrate, but a specific inhibitor, of the APC(Cdh1) complex.
Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA.
Judy Qiju
JQ
Wu
Sally
S
Kornbluth
D064173:Anaphase-Promoting Complex-Cyclosome; D064199:Cdc20 Proteins; D064200:Cdh1 Proteins; D018797:Cell Cycle Proteins / Q000378:metabolism; D008938:Mitosis; D012097:Repressor Proteins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D013379:Substrate Specificity; D043743:Ubiquitin-Protein Ligase Complexes / Q000037:antagonists & inhibitors* / Q000378:metabolism*; D054875:Ubiquitination
C516306:Acm1 protein, S cerevisiae; C577495:CDC20 protein, S cerevisiae; C577583:CDH1 protein, S cerevisiae; D064199:Cdc20 Proteins; D064200:Cdh1 Proteins; D018797:Cell Cycle Proteins; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D043743:Ubiquitin-Protein Ligase Complexes; D064173:Anaphase-Promoting Complex-Cyclosome