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Related Concept Videos

Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Cotranslational Protein Translocation01:20

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.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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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Related Experiment Video

Updated: Jun 22, 2026

Delivery of Therapeutic siRNA to the CNS Using Cationic and Anionic Liposomes
10:33

Delivery of Therapeutic siRNA to the CNS Using Cationic and Anionic Liposomes

Published on: July 23, 2016

siRNA delivery using peptide transduction domains.

Akiko Eguchi1, Steven F Dowdy

  • 1Howard Hughes Medical Institute and Department of Cellular and Molecular Medicine, UCSD School of Medicine, 9500 Gilman Drive, La Jolla, CA 92093-0686, USA.

Trends in Pharmacological Sciences
|June 24, 2009
PubMed
Summary

Peptide transduction domains (PTDs) can effectively deliver short interfering RNAs (siRNAs) into cells, overcoming delivery barriers for potential siRNA-based therapies.

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Last Updated: Jun 22, 2026

Delivery of Therapeutic siRNA to the CNS Using Cationic and Anionic Liposomes
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Published on: July 23, 2016

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11:24

Direct Protein Delivery to Mammalian Cells Using Cell-permeable Cys2-His2 Zinc-finger Domains

Published on: March 25, 2015

Area of Science:

  • Biotechnology
  • Molecular Biology
  • Drug Delivery

Background:

  • Short interfering RNAs (siRNAs) show therapeutic promise but face cellular delivery challenges due to their size and charge.
  • Existing siRNA delivery systems require enhancement for improved cellular uptake.
  • Peptide transduction domains (PTDs) are known for their ability to cross cell membranes independently.

Purpose of the Study:

  • To review the use of PTDs for in vitro and in vivo siRNA delivery.
  • To discuss the potential of PTD-mediated siRNA delivery in therapeutic applications.

Main Methods:

  • Review of existing literature on PTDs and siRNA delivery.
  • Analysis of in vitro and in vivo studies utilizing PTD-siRNA conjugates.
  • Discussion of PTD mechanisms for cellular membrane translocation.

Main Results:

  • PTDs facilitate the cellular entry of siRNAs, overcoming natural membrane barriers.
  • PTDs have been successfully employed for delivering various molecules, including nucleic acids.
  • Studies demonstrate the in vitro and in vivo applicability of PTD-mediated siRNA delivery.

Conclusions:

  • PTDs represent a promising strategy for enhancing siRNA delivery and cellular uptake.
  • PTD-based systems offer potential for advancing siRNA-based therapeutic strategies.
  • Further research into PTD-siRNA systems could lead to novel disease treatments.