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Related Concept Videos

Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

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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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.
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Golgi Apparatus

As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.The Golgi apparatus is a major sorting and dispatch station for the products of the ER. Newly arriving vesicles enter...
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COP Coated Vesicles00:59

COP Coated Vesicles

Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of different...
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Nuclear Protein Sorting

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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Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
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pH-dependent cargo sorting from the Golgi.

Chunjuan Huang1, Amy Chang

  • 1Department of Molecular, Cellular & Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA.

The Journal of Biological Chemistry
|January 18, 2011
PubMed
Summary
This summary is machine-generated.

Loss of vacuolar proton-translocating ATPase (V-ATPase) activity causes missorting of proteins from the Golgi to the vacuole. This pH-dependent mislocalization affects multiple cargo types in yeast secretory pathways.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The vacuolar proton-translocating ATPase (V-ATPase) is crucial for organelle acidification and cellular pH homeostasis.
  • V-ATPase functions alongside other ion transporters in maintaining cellular pH balance.

Purpose of the Study:

  • To investigate the role of V-ATPase activity in protein trafficking within the yeast secretory pathway.
  • To determine the impact of V-ATPase deficiency on the sorting of plasma membrane and Golgi resident proteins.

Main Methods:

  • Analysis of protein missorting in yeast cells with deleted V-ATPase subunits or under glucose deprivation.
  • Utilizing genetic approaches and pH manipulation to assess protein trafficking.
  • Investigating the involvement of Gga adaptors in protein mislocalization.

Main Results:

  • V-ATPase deficiency leads to the missorting of plasma membrane proteins (Pma1, Can1) and Golgi proteins (Kex2, Vrg4) to the vacuole.
  • Mislocalization of Pma1 to the vacuole is dependent on Gga adaptors, independent of ubiquitination.
  • Restoring normal cell surface targeting of Pma1 in V-ATPase-deficient cells by adjusting external pH suggests a cytosolic pH-dependent mechanism.

Conclusions:

  • V-ATPase activity is essential for the correct sorting of multiple proteins within the yeast secretory pathway.
  • Aberrant cytosolic pH resulting from V-ATPase dysfunction causes missorting of distinct cargo proteins.
  • Multiple cargo sorting events at the Golgi apparatus exhibit pH dependence.