DCP1A

Official Full Name

decapping mRNA 1A

Organism

Homo sapiens

GeneID

55802

Background

Decapping is a key step in general and regulated mRNA decay. The protein encoded by this gene is a decapping enzyme. This protein and another decapping enzyme form a decapping complex, which interacts with the nonsense-mediated decay factor hUpf1 and may be recruited to mRNAs containing premature termination codons. This protein also participates in the TGF-beta signaling pathway. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Feb 2014]

Synonyms

SMIF; SMAD4IP1; HSA275986; Nbla00360;

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Detailed Information

The Decapping Methyltransferase 1A (DCP1A) gene encodes a protein that plays a crucial role in the regulation of mRNA stability and translation efficiency.

Structure And Function of DCP1A

The DCP1A protein is highly conserved across various species, including humans, mice, and yeast. The protein consists of two distinct domains: the N-terminal domain is responsible for mRNA binding, while the C-terminal domain contains the catalytic center for mRNA decapping. The N-terminal domain typically consists of two alpha-helical structures (alpha1 and alpha2) and a beta-sheet structure (beta1), which are responsible for binding to the 5'-cap structure of mRNA. The C-terminal domain contains a conserved catalytic core, which is essential for the removal of the 5'-cap through a methyltransferase activity. DCP1A is a member of the conserved decapping enzyme family, which is involved in the degradation of mRNA through the removal of the 5'-cap structure. The 5'-cap is a crucial element that mediates the stability and translation efficiency of mRNA, and its removal leads to the rapid degradation of mRNA by nuclear acid exonuclease.

Role of DCP1A in Cellular Processes

DCP1A plays a critical role in various cellular processes, including mRNA degradation, regulation of gene expression, and cell differentiation. In mRNA degradation, DCP1A interacts with the 5'-cap structure of mRNA and removes the cap through its methyltransferase activity. This process is crucial for the regulation of mRNA stability and translation efficiency, as it allows the cell to control the expression of specific genes at different time points.

DCP1A Regulates Gene Expression

DCP1A also plays a role in the regulation of gene expression through its interaction with chromatin-modifying enzymes. For example, DCP1A has been shown to interact with the histone methyltransferase SET1A, which is responsible for the methylation of lysine 4 on histone 3 (H3K4me1). This interaction leads to the recruitment of other chromatin-modifying enzymes, such as RNA polymerase II, and the activation of gene transcription. In addition to its role in mRNA degradation and gene expression regulation, DCP1A has also been implicated in cell differentiation. For instance, studies have shown that DCP1A is highly expressed in neurons compared to other cell types.

Mechanisms of DCP1A-mediated mRNA Degradation

DCP1A mediates mRNA degradation through its methyltransferase activity, which leads to the removal of the 5'-cap structure from mRNA. The 5'-cap is a crucial element that mediates the stability and translation efficiency of mRNA, and its removal leads to the rapid degradation of mRNA by nuclear acid exonuclease. The methyltransferase activity of DCP1A is responsible for the transfer of a methyl group from the 5'-cap to a specific residue in the mRNA, leading to the disruption of the cap structure and subsequent degradation of the mRNA.

In conclusion, DCP1A is a crucial enzyme that plays a significant role in the regulation of mRNA stability and translation efficiency. DCP1A is also involved in the regulation of gene expression and cell differentiation, making it a key player in various cellular processes.

References:

Wu, Chuanqing et al. "Overexpression of mRNA-decapping enzyme 1a affects survival rate in colorectal carcinoma." Oncology letters vol. 16,1 (2018): 1095-1100. doi:10.3892/ol.2018.8730
Dougherty, Jonathan D et al. "mRNA decapping enzyme 1a (Dcp1a)-induced translational arrest through protein kinase R (PKR) activation requires the N-terminal enabled vasodilator-stimulated protein homology 1 (EVH1) domain." The Journal of biological chemistry vol. 289,7 (2014): 3936-49. doi:10.1074/jbc.M113.518191

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