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Related Concept Videos

RNA Splicing01:32

RNA Splicing

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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...
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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.
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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In eukaryotic cells, nascent mRNA transcripts need to undergo many post-transcriptional modifications to reach the cell cytoplasm and translate into functional proteins. For a long time, transcription and pre-mRNA processing were considered two independent events that occur sequentially in the cell. However, it has now been well established that transcription and pre-mRNA processing are two simultaneous processes that are precisely regulated inside the cell.
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Regulation of the Unfolded Protein Response01:31

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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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Related Experiment Video

Updated: Sep 12, 2025

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
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Functional Differences Between SIRPα Splice Isoforms.

Mihoko Kajita1, Yojiro Matsui1, Kotaro Sugimoto1

  • 1Department of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, Kyoto, Japan.

Genes to Cells : Devoted to Molecular & Cellular Mechanisms
|August 5, 2025
PubMed
Summary
This summary is machine-generated.

Short signal regulatory protein-alpha (SIRPα) binds CD47 but does not inhibit phagocytosis, unlike its long form. Its expression decreases after endotoxin stimulation, suggesting a regulatory role in the "don't eat me" signal.

Keywords:
CD47SIRPαmacrophagephagocytosissplice isoform“don't eat me” signal

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Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • Signal regulatory protein-alpha (SIRPα) is an inhibitory receptor on macrophages, crucial for the
  • don't eat me
  • signal mediated by its ligand, CD47.
  • SIRPα exists in multiple splice isoforms, with functional studies primarily focusing on the long isoform.

Purpose of the Study:

  • To investigate the expression and function of the short SIRPα isoform.
  • To compare the phagocytosis-inhibiting capabilities of short SIRPα versus long SIRPα.

Main Methods:

  • Analysis of short and long SIRPα mRNA expression in Raw 264.7 cells.
  • Assessment of short SIRPα binding to CD47.
  • Evaluation of phagocytosis assays using CD47-coated beads.

Main Results:

  • Short and long SIRPα mRNA levels were comparable in resting macrophages.
  • Endotoxin stimulation significantly decreased the proportion of short SIRPα mRNA.
  • Short SIRPα bound CD47 but failed to suppress phagocytosis, unlike long SIRPα.

Conclusions:

  • Short SIRPα exhibits distinct expression patterns and functional properties compared to long SIRPα.
  • Short SIRPα may act as a modulator of the CD47-mediated "don't eat me" signal.