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Related Concept Videos

Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

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Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation.  In gated transport, folded...
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Regulation of Nuclear Protein Sorting01:45

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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Mitochondrial Protein Sorting01:39

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Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
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Protein Transport to the Thylakoids01:22

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Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
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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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The Early Endosome: Endocytosis of Transferrin01:28

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Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
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Analyzing the Function of Small GTPases by Microinjection of Plasmids into Polarized Epithelial Cells
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A Size Filter Regulates Apical Protein Sorting.

Christian de Caestecker1, Ian G Macara1

  • 1Department of Cell and Developmental Biology, Vanderbilt University School of Medicine; Nashville TN 37205, U.S.

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Summary
This summary is machine-generated.

A size barrier at the trans-Golgi network (TGN) helps sort proteins to the cell

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Area of Science:

  • Cell biology
  • Molecular biology
  • Biochemistry

Background:

  • Apical sorting of epithelial membrane proteins is crucial for cell function but remains poorly understood.
  • Apical proteins typically have smaller cytoplasmic domains than basolateral proteins, but the underlying mechanism is unclear.

Approach:

  • Investigated a potential size barrier at the trans-Golgi network (TGN) for apical protein sorting.
  • Utilized a streptavidin-binding peptide system to control protein release from the endoplasmic reticulum (ER).
  • Examined the role of Crb3 and Ace2 as model apical proteins and their interaction with Pals1.

Key Points:

  • Increasing cytoplasmic bulk of apical proteins significantly delayed their departure from the Golgi.
  • Super-resolution imaging revealed spatial segregation of Crb3 variants within the Golgi.
  • Pals1 dissociation from Crb3 is necessary for timely apical sorting, as a non-dissociable Pals1 mutant hindered Crb3 exit.

Conclusions:

  • An unexpected size filter mechanism at the TGN facilitates the apical sorting of proteins with small cytoplasmic domains.
  • Timely dissociation of Pals1 from Crb3 is essential for regulating Crb3's cytoplasmic domain size and ensuring normal apical sorting kinetics.