Publications by authors named "Stacy L Erickson"

3 Publications

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Competition between Decapping Complex Formation and Ubiquitin-Mediated Proteasomal Degradation Controls Human Dcp2 Decapping Activity.

Mol Cell Biol 2015 Jun 13;35(12):2144-53. Epub 2015 Apr 13.

Division of Biological Sciences, University of California San Diego, La Jolla, California, USA Department of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, Colorado, USA

mRNA decapping is a central step in eukaryotic mRNA decay that simultaneously shuts down translation initiation and activates mRNA degradation. A major complex responsible for decapping consists of the decapping enzyme Dcp2 in association with decapping enhancers. An important question is how the activity and accumulation of Dcp2 are regulated at the cellular level to ensure the specificity and fidelity of the Dcp2 decapping complex. Here, we show that human Dcp2 levels and activity are controlled by a competition between decapping complex assembly and Dcp2 degradation. This is mediated by a regulatory domain in the Dcp2 C terminus, which, on the one hand, promotes Dcp2 activation via decapping complex formation mediated by the decapping enhancer Hedls and, on the other hand, targets Dcp2 for ubiquitin-mediated proteasomal degradation in the absence of Hedls association. This competition between Dcp2 activation and degradation restricts the accumulation and activity of uncomplexed Dcp2, which may be important for preventing uncontrolled decapping or for regulating Dcp2 levels and activity according to cellular needs.
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http://dx.doi.org/10.1128/MCB.01517-14DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4438239PMC
June 2015

Cytoplasmic mRNP granules at a glance.

J Cell Sci 2011 Feb;124(Pt 3):293-7

Division of Biology, University of California San Diego, La Jolla, CA 92093, USA.

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http://dx.doi.org/10.1242/jcs.072140DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3021993PMC
February 2011

A mitotic topoisomerase II checkpoint in budding yeast is required for genome stability but acts independently of Pds1/securin.

Genes Dev 2006 May;20(9):1162-74

Department of Genetics, Cell Biology and Development, University of Minnesota Medical School, Minneapolis, Minnesota 55455, USA.

Topoisomerase II (Topo II) performs topological modifications on double-stranded DNA molecules that are essential for chromosome condensation, resolution, and segregation. In mammals, G2 and metaphase cell cycle delays induced by Topo II poisons have been proposed to be the result of checkpoint activation in response to the catenation state of DNA. However, the apparent lack of such controls in model organisms has excluded genetic proof that Topo II checkpoints exist and are separable from the conventional DNA damage checkpoint controls. But here, we define a Topo II-dependent G2/M checkpoint in a genetically amenable eukaryote, budding yeast, and demonstrate that this checkpoint enhances cell survival. Conversely, a lack of the checkpoint results in aneuploidy. Neither DNA damage-responsive pathways nor Pds1/securin are needed for this checkpoint. Unusually, spindle assembly checkpoint components are required for the Topo II checkpoint, but checkpoint activation is not the result of failed chromosome biorientation or a lack of spindle tension. Thus, compromised Topo II function activates a yeast checkpoint system that operates by a novel mechanism.
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http://dx.doi.org/10.1101/gad.1367206DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1472475PMC
May 2006