Proteomics

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Ubiquitome analysis of UHRF1 and UHRF2-deficient mESCs

ABSTRACT: The E3 ligase UHRF1 is an essential epigenetic cofactor for DNMT1 dependent maintenance DNA methylation, which provides a binding platform for DNMT1 by both cooperative binding of histones and hemi-methylated DNA as well as by ubiquitinating histone H3. Here, we conduct a comprehensive screen to identify novel ubiquitination targets of UHRF1 and its paralogue UHRF2 by comparing the ubiquitome of wildtype (wt), UHRF1- and UHRF2-deficient mouse embryonic stem cells. With an antibody-dependent enrichment of ubiquitin remnant motif-containing peptides followed by isobaric-labeling based quantitative mass spectrometry, we find both known and novel E3 ligase substrates of UHRF1 involved in a variety of biological processes such as RNA processing, DNA methylation and DNA damage repair.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Stem Cell, Cell Culture

SUBMITTER: Elisabeth Karg  

LAB HEAD: Heinrich Leonhardt

PROVIDER: PXD006593 | Pride | 2017-10-24

REPOSITORIES: Pride

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Action DRS
MS_rawfile_details.xlsx Xlsx
Ref1028_ES_20170220_U1r1.raw Raw
Ref1028_ES_20170220_U1r2.raw Raw
Ref1028_ES_20170220_U1r3.raw Raw
Ref1028_ES_20170220_U1r4.raw Raw
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Publications

Indications for angiography in the preoperative evaluation of patients with prolactin-secreting pituitary adenomas.

Richmond I L IL   Newton T H TH   Wilson C B CB  

Journal of neurosurgery 19800301 3

The preoperative angiograms of 100 patients subsequently undergoing transsphenoidal exploration for prolactin-secreting pituitary adenomas were reviewed in order to assess both the risk of this study and its yield of useful diagnostic information. In these patients with documented hyperprolactinemia, no vascular anomalies contraindicating a transsphenoidal approach were detected. Tumor blush was evident only in large tumors. The appearance of lateral displacement of the carotid siphon in basilar  ...[more]

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