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Related Concept Videos

Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

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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...
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The Inner Mitochondrial Membrane01:28

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The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
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Protein Transport to the Inner Chloroplast Membrane01:18

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Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
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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.
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,...
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Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
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Golgi Apparatus01:09

Golgi Apparatus

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Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
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Related Experiment Video

Updated: May 5, 2026

Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

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Destination: inner nuclear membrane.

Santharam S Katta1, Christine J Smoyer1, Sue L Jaspersen2

  • 1Stowers Institute for Medical Research, Kansas City, MO 64110, USA.

Trends in Cell Biology
|November 26, 2013
PubMed
Summary
This summary is machine-generated.

Investigating inner nuclear membrane (INM) protein transport reveals complex pathways. Understanding these mechanisms is crucial for nuclear organization in both healthy and diseased cells.

Keywords:
LEM domainNPCSUN proteininner nuclear membranenuclear transport

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • The inner nuclear membrane (INM) is vital for nuclear structure, chromosome organization, DNA repair, and gene transcription.
  • Mislocalization of INM proteins is linked to various human diseases, but their transport mechanisms remain unclear.

Purpose of the Study:

  • To review and synthesize current knowledge on the targeting pathways of INM proteins.
  • To elucidate the mechanisms governing INM protein localization in eukaryotic cells.

Main Methods:

  • Review of literature on INM protein composition and targeting.
  • Analysis of conserved INM protein pathways across different model systems.
  • Examination of viral and signaling complex nuclear transport.

Main Results:

  • INM transport involves both nuclear pore complex-dependent and -independent pathways.
  • Diverse biological systems offer insights into conserved INM protein targeting mechanisms.
  • Viral and signaling complex transport provide models for understanding INM localization.

Conclusions:

  • Understanding INM targeting pathways is essential for comprehending nuclear organization.
  • Knowledge of INM transport is critical for both normal cellular function and disease pathogenesis.