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Related Concept Videos

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...
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Botulism01:22

Botulism

Botulism is a life-threatening neuroparalytic condition caused by botulinum neurotoxin, which is produced by the bacterium Clostridium botulinum, a Gram-positive, spore-forming, obligate anaerobe.In adults, the toxin enters the body in different ways: in foodborne botulism, the preformed toxin is absorbed in the intestine. In wound botulism, spores grow in injured tissue and release the toxin into the blood. Infant botulism differs mechanistically from adult forms. In infants, botulism commonly...
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...

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Related Experiment Video

Updated: Jul 6, 2026

Reconstitution of Actin-Based Motility with Commercially Available Proteins
08:40

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Published on: October 28, 2022

Actin-binding toxin "tail" wags the dog.

Junichi Tanaka1, J Craig Blain, John S Allingham

  • 1Department of Chemistry, Biology, and Marine Science, University of the Ryukyus, Okinawa 903-0213, Japan.

Chemistry & Biology
|March 22, 2008
PubMed
Summary

Marine macrolides are diverse actin-binding compounds. A study reveals their "tail" side chain is crucial for cytotoxicity, impacting cell function.

Area of Science:

  • Marine natural products
  • Chemical biology
  • Molecular pharmacology

Background:

  • Actin-binding marine macrolides display varied structures and functions.
  • The aliphatic side chain, or
  • tail
  • is a conserved feature in many macrolides.

Discussion:

  • Perrins et al. identify the "tail" as the key determinant of cytotoxicity in marine macrolides.
  • This finding clarifies the structure-activity relationship for these compounds.

Key Insights:

  • The stereochemically conserved aliphatic side chain is essential for the cytotoxic activity of marine macrolides.
  • Cytotoxicity is directly linked to the presence and structure of the macrolide "tail".

Outlook:

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Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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  • Further research can explore modifying the "tail" to develop novel therapeutic agents.
  • Understanding this mechanism may lead to new strategies for drug discovery from marine sources.