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Related Concept Videos

Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
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Protein Folding Quality Check in the RER01:29

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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The structure and stability of mRNA molecules regulates gene expression, as mRNAs are a key step in the pathway from gene to protein. In eukaryotes, the half-life of mRNA varies from a few minutes up to several days. mRNA stability is essential in growth and development. The absence of the proteins regulating its stability, such as tristetraprolin in mice, can cause systemic issues, including bone marrow overgrowth, inflammation, and autoimmunity.
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Export of Misfolded Proteins out of the ER01:32

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Oligosaccharide Assembly01:24

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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MALT1 substrate cleavage: what is it good for?

Bahareh Nemati Moud1, Franziska Ober1, Thomas J O'Neill1

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Frontiers in Immunology
|June 12, 2024
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Summary

The CARD-BCL10-MALT1 (CBM) complex regulates immune responses through MALT1 scaffolding and protease functions. Understanding MALT1 substrate cleavage is crucial for immune homeostasis and treating cancers.

Keywords:
API2-MALT1CBM complexMALT1RNA metabolismauto-regulationcell signalingproteasesubstrate cleavage

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Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Signaling

Background:

  • CARD-BCL10-MALT1 (CBM) signalosomes link immune receptors to activation pathways.
  • MALT1 (PCASP1) has dual roles: scaffolding TRAF6 for NF-κB/AP-1 signaling and protease activity via substrate cleavage.
  • Dysregulation of MALT1 functions leads to immune deficiency or autoimmune inflammation.

Purpose of the Study:

  • To summarize known MALT1 substrates and their functions.
  • To elucidate how MALT1 substrate cleavage contributes to CBM complex biological functions.
  • To highlight the need for connecting MALT1 protease roles to specific substrate cleavage in disease.

Main Methods:

  • Literature review and synthesis of existing research on MALT1 substrates.
  • Analysis of identified MALT1 substrates involved in CBM auto-regulation, signaling, transcription, and mRNA stability.
  • Discussion of computational predictions and screening methods for substrate identification.

Main Results:

  • Approximately 20 MALT1 substrates have been identified, targeting diverse cellular processes.
  • MALT1 substrates include regulators of CBM signaling (MALT1, BCL10, CARD10), adhesion (A20, CYLD), transcription (RelB), and mRNA fate (Regnase-1, Roquin-1/2).
  • Cleavage of individual substrates has distinct pathophysiological implications, impacting immune homeostasis and cancer survival.

Conclusions:

  • Balanced MALT1 scaffolding and protease activity are essential for immune homeostasis.
  • MALT1 protease activity is implicated in aggressive lymphomas and solid cancers.
  • Further research is needed to link specific MALT1 substrate cleavage to its pathophysiological roles.