ArticleProtein science : a publication of the Protein Society2012
Caspases cleave and inhibit the microRNA processing protein DiGeorge Critical Region 8.
Article in Protein science : a publication of the Protein Society, 2012. 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, 13 citations in OpenAlex.
- Caspase-mediated cleavage of miRNA processing proteins Drosha, DGCR8, Dicer, and TRBP2 in heat-shocked cells and its inhibition by HSP70 overexpression.Cell stress & chaperones · 2022Article
- Long-term impact of maternal high-fat diet on offspring cardiac health: role of micro-RNA biogenesis.Cell death discovery · 2019Article
- Article
- Cobalt(III) Protoporphyrin Activates the DGCR8 Protein and Can Compensate microRNA Processing Deficiency.Chemistry & biology · 2015Article
- Deciphering the RNA landscape by RNAome sequencing.RNA biology · 2015Article
- The DGCR8 RNA-binding heme domain recognizes primary microRNAs by clamping the hairpin.Cell reports · 2014Article
- Human RNAi pathway: crosstalk with organelles and cells.Functional & integrative genomics · 2014Review
- Processing of microRNA primary transcripts requires heme in mammalian cells.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Phosphorylation of DGCR8 increases its intracellular stability and induces a progrowth miRNA profile.Cell reports · 2013Article
- miR-221/222: promising biomarkers for breast cancer.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2013Review
- Dimerization and heme binding are conserved in amphibian and starfish homologues of the microRNA processing protein DGCR8.PloS one · 2012Article
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6 authors at 1 institution in 1 country.
Funding
Abstract
DGCR8 (DiGeorge Critical Region 8) is an essential microRNA (miRNA) processing protein that recognizes primary transcripts of miRNAs (pri-miRNAs) and triggers their cleavage by the Drosha nuclease. We previously found that Fe(III) heme binds and activates DGCR8. Here we report that in HeLa cells, DGCR8 undergoes two proteolytic events that produce two C-terminal fragments called DGCR8(C1) and DGCR8(C2) , respectively. DGCR8(C2) accumulates during apoptosis and is generated through cleavage by a caspase. The caspase cleavage site is located in the central loop of the heme-binding domain. Cleavage of DGCR8 by caspase-3 in vitro results in loss of the otherwise tightly bound Fe(III) heme cofactor, dissociation of the N- and C-terminal proteolytic fragments, and inhibition of the pri-miRNA processing activity. These results reveal an intrinsic mechanism in the DGCR8 protein that seems to have evolved for regulating miRNA processing via association with Fe(III) heme and proteolytic cleavage by caspases. Decreased expression of miRNAs has been observed in apoptotic cells, and this change was attributed to caspase-mediated cleavage of a down-stream miRNA processing nuclease Dicer. We suggest that both the Drosha and Dicer cleavage steps of the miRNA maturation pathway may be inhibited in apoptosis and other biological processes where caspases are activated.
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