Plakoglobin

A representation of the 3D structure of the protein myoglobin showing turquoise α-helices. This protein was the first to have its structure solved by X-ray crystallography. Toward the right-center among the coils, a prosthetic group called a heme group (shown in gray) with a bound oxygen molecule (red).

Protein that in humans is encoded by the JUP gene.

- Plakoglobin

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Adherens junction

Adherens junctions (or zonula adherens, intermediate junction, or "belt desmosome" ) are protein complexes that occur at cell–cell junctions, cell–matrix junctions in epithelial and endothelial tissues, usually more basal than tight junctions.

Principal interactions of structural proteins at cadherin-based adherens junction. Actin filaments are associated with adherens junctions in addition to several other actin-binding proteins such as vinculin. The head domain of vinculin associates to E-cadherin via α-, β - and γ -catenins. The tail domain of vinculin binds to membrane lipids and to actin filaments.

γ-catenin or gamma-catenin (plakoglobin) binds the catenin-binding region of the cadherin.

Desmosome

Cell structure specialized for cell-to-cell adhesion.

A desmosome.

Desmogleins and the desmocollin Dsc "a" form contain an intracellular cadherin domain, which binds to plakoglobin.

Catenin

Catenins are a family of proteins found in complexes with cadherin cell adhesion molecules of animal cells.

Interactions of structural proteins at cadherin-based adherens junction. The exact means by which cadherins are linked to actin filaments is still under investigation.
Figure 1. β-catenin at cell-to-cell contacts of P19 embryonal carcinoma cells.

γ-catenin

Catenin beta-1

Protein that in humans is encoded by the CTNNB1 gene.

The simplified structure of beta-catenin.
Partners competing for the main binding site on the ARM domain of beta-catenin. The auxiliary binding site is not shown.
Simplified structure of the beta-catenin destruction complex. Note the high proportion of intrinsically disordered segments in the axin and APC proteins.
The moonlighting of beta-catenin.
Beta-catenin level regulation and cancer.

It is a member of the catenin protein family and homologous to γ-catenin, also known as plakoglobin.

Cadherin-1

Protein that in humans is encoded by the CDH1 gene.

Immunohistochemistry for E-cadherin in invasive lobular carcinoma, showing loss of expression in invasive tumor cells (white arrow).

Plakoglobin,

Armadillo repeat

Name of a characteristic, repetitive amino acid sequence of about 40 residues in length that is found in many proteins.

Structure of a generic L-amino acid in the "neutral" form needed for defining a systematic name, without implying that this form actually exists in detectable amounts either in aqueous solution or in the solid state.

Examples of proteins that contain armadillo repeats include β-catenin, α-importin, plakoglobin, adenomatous polyposis coli (APC), and many others.

Adenomatous polyposis coli

Protein that in humans is encoded by the APC gene.

Familial Adenomatous Polyposis of the intestine
Overview of signal transduction pathways involved in apoptosis.

JUP,

MUC1

Mucin encoded by the MUC1 gene in humans.

The three naturally-occurring isotopes of hydrogen. The fact that each isotope has one proton makes them all variants of hydrogen: the identity of the isotope is given by the number of protons and neutrons. From left to right, the isotopes are protium (1H) with zero neutrons, deuterium (2H) with one neutron, and tritium (3H) with two neutrons.

JUP, and

CDH2

Protein that in humans is encoded by the CDH2 gene.

Gregor Mendel

Plakoglobin.

Desmoglein-2

Protein that in humans is encoded by the DSG2 gene.

A representation of the 3D structure of the protein myoglobin showing turquoise α-helices. This protein was the first to have its structure solved by X-ray crystallography. Toward the right-center among the coils, a prosthetic group called a heme group (shown in gray) with a bound oxygen molecule (red).

The cytoplasmic tails of desmosomal cadherins bind to plakoglobin and plakophilins, which bind desmoplakin.