Phosphorylation of ICBP90 by protein kinase A enhances topoisomerase II$alpha; expression

Trotzier, Marie-Aline

doi:10.1016/s0006-291x(04)00998-2

Cited by 3 publications

(3 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Potential Function of Ser-298 Phosphorylation-It has been reported that UHRF1 is phosphorylated by kinases, including CDK1, CDK2, CK2, and PKA, and the phosphorylations regulate the function of UHRF1 (13,(52)(53)(54). For example, our recent study demonstrated that USP7 interacts with and stabilizes UHRF1 in S phase, and the interaction/stabilization is inhibited by Ser-639 (Ser-652 in the longer UHRF1 isoform with a total of 806 amino acids) phosphorylation of UHRF1 by CDK1-cyclin B in M phase (13).…”

Section: Discussionmentioning

confidence: 99%

Structural Insight into Coordinated Recognition of Trimethylated Histone H3 Lysine 9 (H3K9me3) by the Plant Homeodomain (PHD) and Tandem Tudor Domain (TTD) of UHRF1 (Ubiquitin-like, Containing PHD and RING Finger Domains, 1) Protein

Cheng

Yang

Fang

et al. 2013

Journal of Biological Chemistry

109

129

View full text Add to dashboard Cite

Background: UHRF1 is an important epigenetic regulator connecting DNA methylation and histone methylations. Results: PHD-H3 interaction is independent of the TTD, whereas TTD-H3K9me3 interaction the PHD. Conclusion: Both TTD and PHD are essential for specific recognition of H3K9me3 by human UHRF1. Significance: This work reveals how UHRF1 recognizes H3K9me3, which is important for its cellular localization and DNA methylation.

show abstract

Section: Discussionmentioning

confidence: 99%

Structural Insight into Coordinated Recognition of Trimethylated Histone H3 Lysine 9 (H3K9me3) by the Plant Homeodomain (PHD) and Tandem Tudor Domain (TTD) of UHRF1 (Ubiquitin-like, Containing PHD and RING Finger Domains, 1) Protein

Cheng

Yang

Fang

et al. 2013

Journal of Biological Chemistry

109

129

View full text Add to dashboard Cite

show abstract

“…These common alterations in cancer cells imply the biological functions of UHRF1 that are associated with rapid cellular progression and DNA repair processes (13). In fact, decreasing UHRF1 expression suppresses cellular proliferation by inhibiting G1-S transition (7,14,15). Thus, UHRF1 is considered to play an essential role in cellular proliferation.…”

Section: Introductionmentioning

confidence: 99%

UHRF1 expression is upregulated and associated with cellular proliferation in colorectal cancer

et al. 2012

View full text Add to dashboard Cite

Ubiquitin-like with PHD and ring-finger domain 1 (UHRF1) binds to methylated promoters of a number of tumor-suppressor genes, including p16INK4A and p14ARF, by forming complexes with DNA methyltransferases and HDAC1, resulting in the induction of carcinogenesis. Altered UHRF1 expression has been demonstrated in various types of cancers. Previous reports indicate that UHRF1 expression is regulated by E2F-1 expression. We investigated UHRF1 expression using immunohistochemical staining in 231 colorectal cancer and 40 adenoma specimens, analyzed the relationship between UHRF1 expression and clinicopathological findings and the association between UHRF1 and E2F-1 expression. To better understand the biological function of UHRF1 in colorectal cancer, knockdown of UHRF1 expression was performed using siRNA methods. High UHRF1 expression was observed in 152 of 231 (65.8%) colorectal cancer patients, and was detected in 35 of 40 adenoma specimens samples (87.5%). UHRF1 staining was detected in the nucleus of cancer cells, while it was not detected in colonic normal mucosa. High UHRF1 expression was significantly observed in right compared with left hemicolon cancer (p=0.008). Moreover, high UHRF1 expression tended to be associated with depth of invasion (p=0.051). UHRF1 expression was significantly associated with E2F-1 expression (p<0.0001). Knockdown of UHRF1 expression suppressed cellular growth in colon cancer cell lines, HCT116 and SW620. In conclusion, we demonstrated that UHRF1 expression was upregulated in approximately two-thirds of colorectal cancer specimens and was particularly expressed in right compared with left hemicolon cancer. Moreover, knockdown of UHRF1 expression induced growth inhibition in colon cancer cell lines. UHRF1 may be involved in cellular proliferation and molecular pathogenesis of colorectal cancer in the right hemicolon.

show abstract

“…Protein kinase A directly phosphorylates UHRF1 in response to forskolin-induced cyclic AMP (cAMP) signaling (35). In order to determine if this activation is sufficient to overcome the regeneration defect in our top2a heterozygotes, we challenged hi3635 heterozygotes with the cAMP-activating drug forskolin.…”

Section: Resultsmentioning

confidence: 99%

Topoisomerase IIα Is Required for Embryonic Development and Liver Regeneration in Zebrafish

Dovey

Patton

Bowman

et al. 2009

Molecular and Cellular Biology

View full text Add to dashboard Cite

Topoisomerases solve the topological problems encountered by DNA throughout the lifetime of a cell. Topoisomerase II␣, which is highly conserved among eukaryotes, untangles replicated chromosomes during mitosis and is absolutely required for cell viability. A homozygous lethal mutant, can4, was identified in a screen to identify genes important for cell proliferation in zebrafish by utilizing an antibody against a mitosis-specific marker, phospho-histone H3. Mutant embryos have a decrease in the number of proliferating cells and display increases in DNA content and apoptosis, as well as mitotic spindle defects. Positional cloning revealed that the genetic defect underlying these phenotypes was the result of a mutation in the zebrafish topoisomerase II␣ (top2a) gene. top2a was found to be required for decatenation but not for condensation in embryonic mitoses. In addition to being required for development, top2a was found to be a haploinsufficient regulator of adult liver regrowth in zebrafish. Regeneration analysis of other adult tissues, including fins, revealed no heterozygous phenotype. Our results confirm a conserved role for TOP2A in vertebrates as well as a dose-sensitive requirement for top2a in adults.The accurate and complete replication and separation of chromosomes during mitosis is vital for the viability of cells. One potential complication encountered during cell division is the topological and tensional pressures put on DNA during these processes. Topoisomerases are responsible for enzymatically winding, unwinding, knotting, and unknotting reactions that are necessary for solving the topological problems of DNA. Genetic and biochemical studies in bacteria and yeast have revealed two classes of topoisomerases, type I and type II (38). Type I topoisomerases act on DNA by creating a temporary single-strand nick in DNA, passing the intact strand through the broken strand and then religating the nick. Type II topoisomerases, alternatively, function by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand.During DNA replication, sister chromatids become tangled with each other as a by-product of their duplication. The primary cellular function of type II topoisomerases during mitosis is the decatenation (untangling) of sister chromatids. Consistent with this essential role, genetic studies Saccharomyces cerevisiae have revealed that temperature-sensitive topoisomerase II mutants (TOP2) are unviable at nonpermissive temperatures (10,16,36). These mutants arrest during M phase due to their incompletely decatenated chromatids.Humans have two TOP2 homologues, topoisomerase II alpha (TOP2A) and topoisomerase II beta (TOP2B). Although they are both functionally redundant with the yeast homologue, TOP2A and TOP2B are genetically unique. As the products of different loci, TOP2A and TOP2B have different expression patterns. Specifically, TOP2A expression peaks during M phase, wh...

show abstract

Phosphorylation of ICBP90 by protein kinase A enhances topoisomerase II$alpha; expression

Cited by 3 publications

References 0 publications

Structural Insight into Coordinated Recognition of Trimethylated Histone H3 Lysine 9 (H3K9me3) by the Plant Homeodomain (PHD) and Tandem Tudor Domain (TTD) of UHRF1 (Ubiquitin-like, Containing PHD and RING Finger Domains, 1) Protein

Structural Insight into Coordinated Recognition of Trimethylated Histone H3 Lysine 9 (H3K9me3) by the Plant Homeodomain (PHD) and Tandem Tudor Domain (TTD) of UHRF1 (Ubiquitin-like, Containing PHD and RING Finger Domains, 1) Protein

UHRF1 expression is upregulated and associated with cellular proliferation in colorectal cancer

Topoisomerase IIα Is Required for Embryonic Development and Liver Regeneration in Zebrafish

Contact Info

Product

Resources

About