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Related Concept Videos

Attachment of Sister Chromatids02:57

Attachment of Sister Chromatids

As cells progress into mitosis, the nuclear envelope breaks down, and the condensed chromosomes are exposed to the array of bipolar microtubules of the mitotic spindle. The kinetochore, a large, disc-shaped protein complex, is present at the centromere region of the sister chromatids and acts as a binding site for the microtubules.  Usually, the plus-end of a single microtubule is embedded within the kinetochore. However, some kinetochores first establish lateral contact with the side-wall of a...
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate filaments...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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...
Cytoskeletal Accessory Proteins01:13

Cytoskeletal Accessory Proteins

The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.

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Updated: May 23, 2026

Tension Gauge Tether Probes for Quantifying Growth Factor Mediated Integrin Mechanics and Adhesion
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Published on: February 11, 2022

Structural basis of tetherin function.

Winfried Weissenhorn1, Nolwenn Miguet, Nick Aschman

  • 1Unit of Virus Host Cell Interactions (UVHCI) UMI 3265 Universite Joseph Fourier-EMBL-CNRS, 6 rue Jules Horowitz, 38042 Grenoble Cedex 9, France. weissenhorn@embl.fr

Current HIV Research
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Human cells use tetherin to block HIV-1 replication. However, the virus

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Area of Science:

  • Virology
  • Cell Biology
  • Immunology

Background:

  • Human immunodeficiency virus type 1 (HIV-1) assembly and budding rely on viral structural proteins and host cell factors.
  • Interferon-inducible restriction factors, like tetherin, serve as a primary defense against viral propagation.
  • Enveloped viruses, including HIV-1, have evolved viral antagonists, such as Vpu, to counteract host restriction factors.

Purpose of the Study:

  • To review recent advancements in understanding the dynamic structural properties of tetherin.
  • To elucidate how tetherin's structural characteristics enable it to physically restrain HIV-1.
  • To explain the mechanism by which tetherin bridges viral and cellular membranes during or after budding.

Main Methods:

  • Literature review of recent scientific publications.
  • Analysis of studies focusing on tetherin structure and function.
  • Examination of research on HIV-1 Vpu antagonism of tetherin.

Main Results:

  • Tetherin functions by physically bridging the host plasma membrane and the virion envelope.
  • The dynamic structural properties of tetherin are crucial for its virion retention capability.
  • HIV-1 Vpu antagonizes tetherin, diminishing its restriction and facilitating viral release.

Conclusions:

  • Understanding tetherin's dynamic structure is key to its anti-HIV-1 mechanism.
  • Viral countermeasures like Vpu highlight the ongoing evolutionary arms race between viruses and host defenses.
  • Further research into tetherin's structural dynamics may reveal new therapeutic targets against HIV-1.