Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Catenins

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the...

Tension Response at Adherens Junctions

Tension Response at Adherens Junctions

The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...

Cadherins in Tissue Organization

Cadherins in Tissue Organization

The cadherins are a superfamily of cell adhesion molecules comprising over 180 variants, with specific tissues expressing a particular combination of cadherin types. Cadherins generally exhibit homophilic binding; i.e., cadherins on one cell bind to cadherins of the same or closely related type on another cell. Thus, cells of the same type have a specific affinity to bind to each other and sort themselves into clusters to form tissues.
Cell Sorting During Development
Cell sorting plays an...

Structural Protein Function

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...

Structural Protein Function

Structural Protein Function

Cytoskeletal Accessory Proteins

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

SpyCEP dismantles neutrophil immunity via disorder-driven chemokine remodeling and GAG targeting.

Proceedings of the National Academy of Sciences of the United States of America·2026

Same author

Evidence for a Two-Step Model for Activation of GPR25 by the Chemoattractant CXCL17.

Basic & clinical pharmacology & toxicology·2026

Same author

TSP-1 interaction with RANK and OPG: implications for bone remodeling and osteolytic bone metastasis.

Cell death & disease·2026

Same author

Synovial matrix turnover controls immune cell spatial patterning in inflammation resolution.

Molecular systems biology·2025

Same author

Investigating endogenous immune-mediated monocyte memory in rheumatoid arthritis.

Annals of the rheumatic diseases·2025

Same author

Remodelling of the immune landscape by IFNγ counteracts IFNγ-dependent tumour escape in mouse tumour models.

Nature communications·2025

Search research articles

Related Experiment Video

Updated: Apr 19, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

Tenascin-C: Form versus function.

Sean P Giblin¹, Kim S Midwood

¹a Nuffield Department of Orthopaedics; Rheumatology and Musculoskeletal Sciences ; Kennedy Institute of Rheumatology; University of Oxford ; Oxford , UK.

Cell Adhesion & Migration

|December 9, 2014

Summary

Understanding tenascin-C (a versatile extracellular matrix protein) requires studying its diverse functions and expression patterns. Post-transcriptional and post-translational modifications are crucial for defining tenascin-C

Keywords:

AD1/AD2, additional domain 1/ additional domain 2 ADAMTS, a disintegrin and metalloproteinase with thrombospondin motifs ASMCs, aortic smooth muscle cells BDNF, brain derived neurotrophic factor BHKs, baby hamster kidney cells BMP, bone morphogenetic protein CA19–9, carbohydrate antigen 19–9 CALEB, chicken acidic leucine-rich EGF-like domain containing brain protein CEA, carcinoembryonic antigen CNS, central nervous system CRC, colorectal carcinomas CTGF, connective tissue growth factor DCIS, ductal carcinoma in-situ ECM, extracellular matrix EDA-FN, extra domain A containing fibronectin EDB-FN, extra domain B containing fibronectin EGF-L, epidermal growth factor-like EGF-R, epidermal growth factor receptor ELISPOT, enzyme-linked immunospot assay FBG, fibrinogen-like globe FGF2, fibroblast growth factor 2 FGF4, fibroblast growth factor 4 FN, fibronectin FNIII, fibronectin type III-like repeat GMEM, glioma-mesenchymal extracellular matrix antigen GPI, glycosylphosphatidylinositol HB-EGF, heparin-binding EGF-like growth factor HCEs, immortalized human corneal epithelial cell line HGF, hepatocyte growth factor HNK-1, human natural killer-1 HSPGs, heparan sulfate proteoglycans HUVECs, human umbilical vein endothelial cells ICC, immunocytochemistry IF, immunofluorescence IFNγ, interferon gamma IGF, insulin-like growth factor IGF-BP, insulin-like growth factor-binding protein IHC, immunohistochemistry IL, interleukin ISH, in situ hybridization LPS, lipopolysaccharide MMP, matrix metalloproteinase MPNSTs, malignant peripheral nerve sheath tumors Mr, molecular mass NB, northern blot NF-kB, nuclear factor kappa-light-chain-enhancer of activated B cells NK, natural killer cells NSCLC, non-small cell lung carcinoma NSCs, neural stem cells NT, neurotrophin PAMPs, pathogen-associated molecular patterns PDGF, platelet derived growth factor PDGF-Rβ, platelet derived growth factor receptor β PIGF, phosphatidylinositol-glycan biosynthesis class F protein PLCγ, phospholipase-C gamma PNS, peripheral nervous system PTPRζ1, receptor-type tyrosine-protein phosphatase zeta RA, rheumatoid arthritis RCC, renal cell carcinoma RD, rhabdomyosarcoma RGD, arginylglycylaspartic acid RT-PCR, real-time polymerase chain reaction SB, Southern blot SCC, squamous cell carcinoma SMCs, smooth muscle cells SVZ, sub-ventricular zone TA, tenascin assembly domain TGFβ, transforming growth factor β TIMP, tissue inhibitor of metalloproteinases TLR4, toll-like receptor 4 TNFα, tumor necrosis factor α TSS, transcription start site UBC, urothelial bladder cancer UCC, urothelial cell carcinoma VEGF, vascular endothelial growth factor VSMCs, vascular smooth muscle cells VZ, ventricular zone WB, immunoblot/ western blot bFGF, basic fibroblast growth factor biosynthesis c, charged cancer ccRCC, clear cell renal cell carcinoma chRCC, chromophobe-primary renal cell carcinoma development glycosylation mAb, monoclonal antibody matrix assembly mitogen-activated protein kinase, MAPK pHo, extracellular pH pRCC, papillary renal cell carcinoma proteolytic cleavage siRNA, small interfering RNA splicing tenascin-C therapeutics transcription

More Related Videos

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells

Published on: September 28, 2020

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Published on: December 20, 2017

Related Experiment Videos

Last Updated: Apr 19, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells

Published on: September 28, 2020

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Published on: December 20, 2017

Area of Science:

Biochemistry
Cell Biology
Molecular Biology

Background:

Tenascin-C is a large, multimodular extracellular matrix glycoprotein.
It displays restricted expression patterns but diverse functions.

Purpose of the Study:

To discuss the importance of understanding tenascin-C expression and function.
To highlight the role of post-transcriptional and post-translational modifications in tenascin-C biology.

Main Methods:

Review of existing literature on tenascin-C.
Analysis of post-transcriptional events (e.g., splicing).
Analysis of post-translational events (e.g., glycosylation, matrix assembly, proteolytic cleavage).

Main Results:

Different forms of tenascin-C arise from various modifications.
These modifications significantly influence tenascin-C's biological activities.
Understanding these modifications is key to fully grasping tenascin-C's role.

Conclusions:

Deciphering tenascin-C expression and function is vital.
Post-transcriptional and post-translational modifications critically define tenascin-C's diverse functions.
Further research into these modifications will advance tenascin-C biology understanding.