Related Experiment Video

Updated: Jun 29, 2026

Detection of Nuclear Blebbing and DNA Leakage in Mammalian Cells by Immunofluorescence
06:23

Detection of Nuclear Blebbing and DNA Leakage in Mammalian Cells by Immunofluorescence

Published on: January 17, 2025

Plectin deficiency affects precursor formation and dynamics of vimentin networks

Radovan Spurny1, Martin Gregor, Maria J Castañón

  • 1Department of Molecular Cell Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter, A-1030 Vienna, Austria.

Experimental Cell Research
|October 14, 2008
PubMed

Insights

Plectin is crucial for vimentin intermediate filament dynamics. It aids in vimentin assembly, motility, and stability, and prevents network disassembly during cell division.

Area of Science:

  • Cell Biology
  • Cytoskeletal Dynamics
  • Protein Interactions

Background:

  • Plectin is a cytolinker protein connecting intermediate filaments to other cytoskeletal systems.
  • Vimentin is a key intermediate filament subunit and a major binding partner of plectin in fibroblasts.
  • Vimentin networks are dynamic, with assembly and disassembly occurring stepwise.

Purpose of the Study:

  • To investigate the role of plectin in the dynamics of vimentin intermediate filament formation.
  • To compare vimentin filament formation in plectin-deficient versus wild-type fibroblasts.

Main Methods:

  • Utilized GFP-tagged vimentin to monitor filament formation in real-time.
  • Studied vimentin and plectin dynamics in spreading and dividing fibroblasts.
  • Compared plectin-deficient and wild-type fibroblast models.

Main Results:

  • Plectin associates with vimentin during early assembly stages.
  • Plectin is essential for vimentin motility and stepwise stable filament formation.
  • Plectin prevents complete vimentin network disassembly during mitosis.

Conclusions:

  • Plectin plays a critical role in regulating vimentin network dynamics, including assembly, motility, and stability.
  • Plectin facilitates the rebuilding of vimentin networks in daughter cells post-mitosis.
  • These findings highlight plectin's importance in maintaining cytoskeletal integrity throughout the cell cycle.

More Related Videos

Aip1p Dynamics Are Altered by the R256H Mutation in Actin08:57

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

Related Concept Videos

Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
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...
Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...