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RNA Splicing

RNA Splicing

Splicing is the process by which eukaryotic RNA is edited before its translation into protein. The RNA strand transcribed from eukaryotic DNA is called the primary transcript. The primary transcripts that become mRNAs are called precursor messenger RNAs (pre-mRNAs). Eukaryotic pre-mRNA contains alternating sequences of exons and introns. Exons are nucleotide sequences that code for proteins, whereas introns are the non-coding regions. In RNA splicing, introns are removed and exons are bonded...

RNA Splicing

RNA Splicing

Alternative RNA Splicing

Alternative RNA Splicing

Alternative RNA splicing is the regulated splicing of exons and introns to produce different mature mRNAs from a single pre-mRNA. Unlike in constitutive splicing where a single gene produces a single type of mRNA, alternative splicing allows an organism to produce multiple proteins from a single gene and plays an important role in protein diversity.
There are five types of alternative RNA splicing that vary in the ways the pre-mRNA segments are removed or retained in the mature mRNA. The first...

Alternative RNA Splicing

Alternative RNA Splicing

Exon Recombination

Exon Recombination

The evolution of new genes is critical for speciation. Exon recombination, also known as exon shuffling or domain shuffling, is an important means of new gene formation. It is observed across vertebrates, invertebrates, and in some plants such as potatoes and sunflowers. During exon recombination, exons from the same or different genes recombine and produce new exon-intron combinations, which might evolve into new genes.
Exon shuffling follows “splice frame rules.” Each exon...

Pre-mRNA Processing: RNA Splicing

Pre-mRNA Processing: RNA Splicing

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Related Experiment Video

Updated: Mar 31, 2026

Detection of Alternative Splicing During Epithelial-Mesenchymal Transition

Detection of Alternative Splicing During Epithelial-Mesenchymal Transition

Published on: October 9, 2014

Alternative splicing generates a novel CARD9 isoform.

Pallavi Juneja¹, Supriya Tanwar¹, Rana Zaidi¹

¹Department of Biochemistry, School of Chemical and Life Sciences, Jamia Hamdard, New Delhi, 110062, India.

|March 29, 2026

Summary

This summary is machine-generated.

Researchers discovered a new CARD9 (Caspase Recruitment Domain Family, member 9) transcript, CARD9-N, impacting innate immunity. This isoform

Keywords:

Alternative splicing CARD9 Fungal pathogenesis Immune response MD simulation

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Last Updated: Mar 31, 2026

Detection of Alternative Splicing During Epithelial-Mesenchymal Transition

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Published on: October 9, 2014

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Identification of Alternative Splicing and Polyadenylation in RNA-seq Data

Identification of Alternative Splicing and Polyadenylation in RNA-seq Data

Published on: June 24, 2021

Area of Science:

Immunology
Molecular Biology
Genetics

Background:

CARD9 (Caspase Recruitment Domain Family, member 9) is crucial for innate immune signaling against pathogens.
CARD9 deficiency compromises host defense, increasing susceptibility to infections.
Understanding CARD9's functional diversity is key to immune regulation.

Purpose of the Study:

To identify and characterize novel CARD9 transcripts.
To investigate the structural and functional differences between CARD9 and its new isoform, CARD9-N.
To explore the potential immune regulatory roles of CARD9-N.

Main Methods:

Integrated bioinformatics and molecular biology techniques were employed.
Structural and functional characterization of the novel CARD9-N transcript.
Analysis of molecular weight, isoelectric point, phosphorylation sites, and dimerization stability.

Main Results:

A novel human CARD9 transcript, CARD9-N, was identified.
CARD9-N possesses a distinct N-terminal region, lacking coding exons E1 and E2 but including a novel N3' sequence.
Significant structural and functional differences observed, including altered dimerization stability and absence of the CARD domain in CARD9-N.

Conclusions:

The novel CARD9-N isoform exhibits unique structural and functional properties compared to CARD9.
The absence of the CARD domain in CARD9-N may lead to distinct immune activation mechanisms.
These findings expand our understanding of CARD9's functional diversity in immune responses and disorders.