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Related Concept Videos

Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
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,...
Receptor-mediated Endocytosis01:20

Receptor-mediated Endocytosis

Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
Clathrin-Mediated Endocytosis of LDL
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Receptor-mediated Endocytosis01:38

Receptor-mediated Endocytosis

Overview
Receptor-Mediated Endocytosis01:20

Receptor-Mediated Endocytosis

Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
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Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...

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Updated: May 28, 2026

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

Outer membrane vesicles hijack TIM-1 for cellular uptake.

Craig R MacNair1, Varnesh Tiku1,2, Shengya Cao3,4

  • 1Infectious Diseases and Host-Microbe Interactions Department, Genentech Inc., San Francisco, California, United States of America.

Plos Pathogens
|May 26, 2026
PubMed
Summary
This summary is machine-generated.

Outer membrane vesicles (OMVs) from bacteria are internalized by host cells through T-cell immunoglobulin and mucin-domain 1 (TIM-1) receptor-mediated endocytosis. This discovery offers new strategies for antivirulence and OMV-based therapies.

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12:48

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Published on: August 21, 2017

Area of Science:

  • Microbiology
  • Cell Biology
  • Immunology

Background:

  • Outer membrane vesicles (OMVs) are bacterial nanoparticles involved in host-pathogen interactions.
  • Mechanisms of OMV entry into host cells are not fully understood.
  • OMVs have potential applications in vaccines and drug delivery.

Purpose of the Study:

  • To elucidate the host cell receptors and mechanisms involved in OMV uptake.
  • To identify specific host factors mediating bacterial OMV internalization.
  • To explore therapeutic strategies targeting OMV-host interactions.

Main Methods:

  • High-throughput screening of human transmembrane proteins for OMV binding.
  • Functional assays including receptor overexpression and knockout.
  • Antibody-mediated blockade of receptor-ligand interactions.
  • Mechanistic studies on receptor-ligand binding and downstream effects.

Main Results:

  • T-cell immunoglobulin and mucin-domain 1 (TIM-1) was identified as a key receptor for E. coli OMV uptake.
  • TIM-1 overexpression enhanced OMV internalization; TIM-1 knockout/blockade reduced it.
  • TIM-1 binds to OMV lipopolysaccharide (LPS) via its phosphatidylserine-binding domain.
  • TIM-1-mediated OMV uptake triggers proinflammatory cytokine production.
  • Multiple bacterial species' OMVs utilize TIM-1 for entry.

Conclusions:

  • TIM-1 is a critical host receptor mediating the uptake of bacterial OMVs.
  • Targeting the TIM-1-OMV interaction can modulate pathogenesis and inflammation.
  • This finding provides a novel approach for developing antivirulence strategies and enhancing OMV-based therapies.