ArticleThe Journal of biological chemistry2011
Terminal uridyltransferase enzyme Zcchc11 promotes cell proliferation independent of its uridyltransferase activity.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Postoperative recurrence of mixed extragonadal germ cell tumor in the right shoulder: a case report.Diagnostic pathology · 2023Article
- CDE-1 suppresses the production of risiRNA by coupling polyuridylation and degradation of rRNA.BMC biology · 2020Article
- Unbiased screen of RNA tailing activities reveals a poly(UG) polymerase.Nature methods · 2019Article
- The RNA uridyltransferase Zcchc6 is expressed in macrophages and impacts innate immune responses.PloS one · 2017Article
- Selective microRNA uridylation by Zcchc6 (TUT7) and Zcchc11 (TUT4).Nucleic acids research · 2014Article
- miR-26a enhances miRNA biogenesis by targeting Lin28B and Zcchc11 to suppress tumor growth and metastasis.Oncogene · 2014Article
- Poly(A) polymerase (PAP) diversity in gene expression--star-PAP vs canonical PAP.FEBS letters · 2014Review
- The nucleic acid-binding domain and translational repression activity of a Xenopus terminal uridylyl transferase.The Journal of biological chemistry · 2013Article
- Regulation of miRNA biogenesis as an integrated component of growth factor signaling.Current opinion in cell biology · 2013Review
- Lin28-mediated control of let-7 microRNA expression by alternative TUTases Zcchc11 (TUT4) and Zcchc6 (TUT7).RNA (New York, N.Y.) · 2012Article
- Zcchc11 uridylates mature miRNAs to enhance neonatal IGF-1 expression, growth, and survival.PLoS genetics · 2012Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Zcchc11 is a uridyltransferase protein with enzymatic activity directed against diverse RNA species. On the basis of its known uridylation targets, we hypothesized that Zcchc11 might regulate cell proliferation. Confirming this, loss-of-function and complementary gain-of-function experiments consistently revealed that Zcchc11 promotes the transition from G(1) to S phase of the cell cycle. This activity takes place through both Rb-dependent and Rb-independent mechanisms by promoting the expression of multiple G(1)-associated proteins, including cyclins D(1) and A and CDK4. Surprisingly, a Zcchc11 construct with point mutations inactivating the uridyltransferase domain enhanced cell proliferation as effectively as wild-type Zcchc11. Furthermore, truncated mutant constructs revealed that the cell cycle effects of Zcchc11 were driven by the N-terminal region of the protein that lacks the RNA-binding domains and uridyltransferase activity of the full protein. Therefore, the N-terminal portion of Zcchc11, which lacks nucleotidyltransferase capabilities, is biologically active and mediates a previously unrecognized role for Zcchc11 in facilitating cell proliferation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.