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Related Concept Videos

Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

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Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
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In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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COP Coated Vesicles00:59

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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...
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Transport Across the Golgi01:26

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While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
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Protein Translocation Machinery on the ER Membrane01:28

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
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Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
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Encapsulin cargo loading: progress and potential.

Jesse A Jones1, Robert Benisch2, Tobias W Giessen1,2

  • 1Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI, USA. tgiessen@umich.edu.

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|May 9, 2023
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Summary

Encapsulins are protein nanocompartments that package specific proteins. Researchers are exploring their use in engineered systems by fusing targeting peptides to new cargo proteins for various applications.

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Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Synthetic Biology

Background:

  • Encapsulins are prokaryotic protein nanocompartments with icosahedral structures (24-42 nm).
  • They self-assemble and selectively encapsulate specific cargo proteins in vivo.
  • Thousands of encapsulin systems exist across bacteria and archaea, classified into four families.

Purpose of the Study:

  • To review current knowledge on cargo protein encapsulation by encapsulins.
  • To highlight engineered systems utilizing targeting peptides for novel applications.

Main Methods:

  • Analysis of encapsulin families and their cargo targeting mechanisms.
  • Review of studies engineering encapsulins with non-native cargo proteins.

Main Results:

  • Cargo encapsulation relies on targeting motifs interacting with the encapsulin shell.
  • Family 1 uses C-terminal targeting peptides (TPs), while Family 2 uses N-terminal targeting domains (TDs).
  • TPs are modular and can be fused to non-native proteins for encapsulation.

Conclusions:

  • Encapsulins offer a versatile platform for nano-compartmentalization.
  • Engineered TP fusions enable creative applications for encapsulin systems.
  • Further research can expand the utility of these protein nanocompartments.