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Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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COP Coated Vesicles00:59

COP Coated Vesicles

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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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Eukaryotic Compartmentalization01:46

Eukaryotic Compartmentalization

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One of the distinguishing features of eukaryotic cells is that they contain membrane-bound organelles, such as the nucleus and mitochondria, that carry out specialized functions. Since biological membranes are only selectively permeable to solutes, they help create a compartment with controlled conditions inside an organelle. These microenvironments are tailored to the organelle's specific functions and help isolate them from the surrounding cytosol.
For example, lysosomes in the animal cells...
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Clathrin Coated Vesicles01:12

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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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Pinocytosis00:38

Pinocytosis

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Cells use energy-requiring bulk transport mechanisms to transfer large particles or large numbers of small particles into or out of the cell. The cells envelop the particles in spherical membranes called vesicles or vacuoles. Vesicles that transport material into the cell are built from the cell membrane. These vesicles encapsulate external molecules and transport them into the cell in a process called endocytosis.
Pinocytosis ("cellular drinking") is one of three main types of...
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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Related Experiment Video

Updated: Sep 16, 2025

In Vitro Reconstitution of the Actin Cytoskeleton Inside Giant Unilamellar Vesicles
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In Vitro Reconstitution of the Actin Cytoskeleton Inside Giant Unilamellar Vesicles

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Encapsulins: catalysis inside a shell.

Asif Fazal1, Tobias W Giessen1

  • 1Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.

Current Opinion in Microbiology
|July 6, 2025
PubMed
Summary
This summary is machine-generated.

Encapsulins are protein shells in prokaryotes that package other proteins, enhancing their stability and function. This review details the catalytic mechanisms and benefits of these encapsulated cargo proteins.

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Last Updated: Sep 16, 2025

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Encapsulins are protein-based nanocompartments found in prokaryotes.
  • They self-assemble into a shell, encapsulating specific cargo proteins.
  • This compartmentalization is crucial for cellular organization and metabolic processes.

Purpose of the Study:

  • To review characterized encapsulin cargo proteins.
  • To elucidate their catalytic mechanisms.
  • To understand the benefits of protein encapsulation within these shells.

Main Methods:

  • Literature review of scientific publications on encapsulins and their cargo.
  • Analysis of biochemical and physiological data on encapsulin systems.
  • Focus on catalytic mechanisms and functional advantages of encapsulated proteins.

Main Results:

  • Encapsulation enhances cargo protein stability and activity.
  • The protein shell acts as a selective diffusion barrier.
  • Encapsulin-cargo systems play roles in homeostasis, storage, and stress resistance.

Conclusions:

  • Encapsulin-cargo systems offer significant advantages for prokaryotic cellular functions.
  • Understanding these systems provides insights into protein compartmentalization and its benefits.
  • Further research into specific cargo proteins can reveal novel biochemical pathways.