Related Experiment Video

Updated: Aug 8, 2026

Nano-fEM: Protein Localization Using Photo-activated Localization Microscopy and Electron Microscopy
13:13

Nano-fEM: Protein Localization Using Photo-activated Localization Microscopy and Electron Microscopy

Published on: December 3, 2012

[Immunogold labeling electron microscopy showing vimentin filament anchored on nuclear pore complex]

S T Cai1, F L Zhou, J Z Zhang

  • 1Institute of Biophysics Academia Sinica, Beijing.

Shi Yan Sheng Wu Xue Bao
|June 1, 1997
PubMed

Insights

Turkey erythrocytes contain vimentin intermediate filaments. These filaments anchor to the nuclear pore complex, suggesting a role in nuclear transport.

Area of Science:

  • Cell Biology
  • Cytoskeletal Dynamics
  • Nuclear Pore Complex Structure

Context:

  • The precise relationship between intermediate filaments and the nucleus remains incompletely understood.
  • Intermediate filaments are crucial cytoskeletal components with diverse cellular roles.
  • The turkey erythrocyte serves as a model system for investigating nuclear-cytoskeletal interactions.

Purpose:

  • To identify the intermediate filament protein in turkey erythrocytes.
  • To determine the localization and anchoring mechanism of these filaments relative to the nucleus.
  • To explore the potential involvement of intermediate filaments in nuclear transport.

Summary:

  • Sequential cell fractionation and immunoblotting identified vimentin as the intermediate filament protein in turkey erythrocytes.
  • Pre-embedment immunogold labeling demonstrated that cytoplasmic intermediate filaments specifically bind anti-vimentin antibodies.
  • These vimentin filaments were found to be anchored to the nuclear pore complex, suggesting a direct physical link.

Impact:

  • This study reveals that vimentin filaments are anchored to the nuclear pore complex in turkey erythrocytes.
  • The findings suggest a novel interaction where vimentin filaments bind to Nup 180, a component of the nuclear pore complex.
  • This interaction implies a potential role for intermediate filaments in regulating nuclear transport processes.

More Related Videos

Nanogold Labeling of the Yeast Endosomal System for Ultrastructural Analyses09:49

Nanogold Labeling of the Yeast Endosomal System for Ultrastructural Analyses

Published on: July 14, 2014

Direct Synthesis of EM-Visible Gold Nanoparticles in Cells for Protein Localization Analysis with Well-Preserved Ultrastructure09:22

Direct Synthesis of EM-Visible Gold Nanoparticles in Cells for Protein Localization Analysis with Well-Preserved Ultrastructure

Published on: April 28, 2023

Related Concept Videos

Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

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...
Golgi Matrix Proteins01:12

Golgi Matrix Proteins

Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
Immunogold Electron Microscopy01:20

Immunogold Electron Microscopy

Immunoelectron microscopy utilizes immunogold labeling of endogenous proteins with specific antibodies to detect and localize these proteins in cells and tissues. The procedure provides insights into the distribution and quantification of protein under different stimulation conditions offering clues about their functions. Conjugating highly electron-dense gold particles with primary or secondary antibodies allow antigen detection on and within cells, with high resolution and specificity.