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Related Concept Videos

Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
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Protein Translocation Machinery on the ER Membrane

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Sec61 protein conducting channel
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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Overview of Protein Sorting and Transport

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Different subcellular localisations of TRIM22 suggest species-specific function.

Anna-Maria Herr1, Ralf Dressel, Lutz Walter

  • 1Department of Primate Genetics, German Primate Center, Göttingen, Germany. aherr@gwdg.de

Immunogenetics
|February 13, 2009
PubMed
Summary

The B30.2/SPRY domain in TRIM22 proteins drives species-specific antiviral activity. Amino acid changes in variable loops 1 and 3 determine distinct subcellular localizations, impacting retroviral resistance.

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Last Updated: Jun 25, 2026

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Area of Science:

  • Immunology
  • Virology
  • Genetics

Background:

  • The B30.2/SPRY domain is crucial for TRIM5alpha's antiviral activity against retroviruses.
  • This domain undergoes rapid evolution in primates, leading to species-specific antiviral functions.
  • TRIM22 is a positively selected TRIM gene with a known antiviral role.

Purpose of the Study:

  • To investigate the role of the B30.2 domain in TRIM22's subcellular localization and antiviral activity.
  • To identify the specific regions within the B30.2 domain responsible for differential localization between human and rhesus TRIM22.

Main Methods:

  • Subcellular localization studies of human and rhesus TRIM22.
  • Analysis of the B30.2 domain's contribution to localization differences.
  • Site-directed mutagenesis to identify key amino acid residues in variable loops (VL1 and VL3).

Main Results:

  • Human and rhesus TRIM22 exhibit distinct subcellular compartment localization.
  • The B30.2 domain is responsible for these observed localization differences.
  • Specific amino acid substitutions in variable loops 1 and 3 of the B30.2 domain dictate subcellular localization.

Conclusions:

  • The rapidly evolving B30.2 domain of TRIM22 influences its subcellular localization.
  • Variations within specific loops of the B30.2 domain contribute to species-specific antiviral defense mechanisms.
  • Understanding these variations is key to elucidating primate-specific retroviral resistance.