Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:6.3.2.19 (
ubiquitin-protein ligase
)
799
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Protein ubiquitylation regulates many cellular processes, including cell division. We report here a novel mutation altering the
Saccharomyces cerevisiae
E1
ubiquitin-activating enzyme
(
uba1-W928R
) that suppresses the temperature sensitivity and chromosome loss phenotype of a well-characterized Aurora B mutant (
ip1-2
). The
uba1-W928R
mutation increases histone H3-S10 phosphorylation in the
ipl1-2
strain, indicating that
uba1-W928R
acts by increasing Ipl1 activity and/or reducing the opposing protein phosphatase 1 (
PP1
; Glc7 in
S. cerevisiae
) phosphatase activity. Consistent with this hypothesis, Ipl1 protein levels and stability are elevated in the
uba1-W928R
mutant, likely mediated via the E2 enzymes Ubc4 and Cdc34. In contrast, the
uba1-W928R
mutation does not affect Glc7 stability, but exhibits synthetic lethality with several
glc7
mutations. Moreover,
uba1-W928R
cells have an altered subcellular distribution of Glc7 and form nuclear Glc7 foci. These effects are likely mediated via the E2 enzymes Rad6 and Cdc34. Our new
UBA1
allele reveals new roles for ubiquitylation in regulating the Ipl1-Glc7 balance in budding yeast. While ubiquitylation likely regulates Ipl1 protein stability via the canonical proteasomal degradation pathway, a non-canonical ubiquitin-dependent pathway maintains normal Glc7 localization and activity.This article has an associated First Person interview with the first author of the paper.
...
PMID:New ubiquitin-dependent mechanisms regulating the Aurora B-protein phosphatase 1 balance in
Saccharomyces cerevisiae
. 3005 82
