CDH3 (gene)

Last updated
CDH3
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases CDH3 , CDHP, HJMD, PCAD, cadherin 3
External IDs OMIM: 114021 MGI: 88356 HomoloGene: 20425 GeneCards: CDH3
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001793
NM_001317195
NM_001317196

NM_001037809
NM_007665

RefSeq (protein)

NP_001304124
NP_001304125
NP_001784

NP_001032898
NP_031691

Location (UCSC) Chr 16: 68.64 – 68.73 Mb Chr 8: 107.24 – 107.28 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Cadherin-3, also known as P-Cadherin, is a protein that in humans is encoded by the CDH3 gene. [5] [6]

Contents

Function

This gene is a classical cadherin from the cadherin superfamily. The encoded protein is a calcium-dependent cell-cell adhesion glycoprotein composed of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. This gene is located in a six-cadherin cluster in a region on the long arm of chromosome 16 that is involved in loss of heterozygosity events in breast and prostate cancer. In addition, aberrant expression of this protein is observed in cervical adenocarcinomas.

Clinical significance

Mutations in this gene have been associated with congenital hypotrichosis with juvenile macular dystrophy. [6]

Interactions

CDH3 (gene) has been shown to interact with:

History

Cadherin-3 was first described in 1986 by Masatoshi Takeichi's laboratory as a new cadherin molecule most abundant in the developing mouse placenta – hence "P-cadherin". [10] [11]

See also

Related Research Articles

<span class="mw-page-title-main">Cadherin</span>

Cadherins (named for "calcium-dependent adhesion") are cell adhesion molecules important in forming adherens junctions that let cells adhere to each other. Cadherins are a class of type-1 transmembrane proteins, and they depend on calcium (Ca2+) ions to function, hence their name. Cell-cell adhesion is mediated by extracellular cadherin domains, whereas the intracellular cytoplasmic tail associates with numerous adaptors and signaling proteins, collectively referred to as the cadherin adhesome.

<span class="mw-page-title-main">Catenin</span>

Catenins are a family of proteins found in complexes with cadherin cell adhesion molecules of animal cells. The first two catenins that were identified became known as α-catenin and β-catenin. α-Catenin can bind to β-catenin and can also bind filamentous actin (F-actin). β-Catenin binds directly to the cytoplasmic tail of classical cadherins. Additional catenins such as γ-catenin and δ-catenin have been identified. The name "catenin" was originally selected because it was suspected that catenins might link cadherins to the cytoskeleton.

<span class="mw-page-title-main">Desmoglein-2</span>

Desmoglein-2 is a protein that in humans is encoded by the DSG2 gene. Desmoglein-2 is highly expressed in epithelial cells and cardiomyocytes. Desmoglein-2 is localized to desmosome structures at regions of cell-cell contact and functions to structurally adhere adjacent cells together. In cardiac muscle, these regions are specialized regions known as intercalated discs. Mutations in desmoglein-2 have been associated with arrhythmogenic right ventricular cardiomyopathy and familial dilated cardiomyopathy.

<span class="mw-page-title-main">Catenin beta-1</span> Mammalian protein found in Homo sapiens

Catenin beta-1, also known as beta-catenin (β-catenin), is a protein that in humans is encoded by the CTNNB1 gene.

<span class="mw-page-title-main">Plakoglobin</span> Mammalian protein found in Homo sapiens

Plakoglobin, also known as junction plakoglobin or gamma-catenin, is a protein that in humans is encoded by the JUP gene. Plakoglobin is a member of the catenin protein family and homologous to β-catenin. Plakoglobin is a cytoplasmic component of desmosomes and adherens junctions structures located within intercalated discs of cardiac muscle that function to anchor sarcomeres and join adjacent cells in cardiac muscle. Mutations in plakoglobin are associated with arrhythmogenic right ventricular dysplasia.

<span class="mw-page-title-main">T-cadherin</span> GPI-anchored signaling protein

T-cadherin, also known as cadherin 13, H-cadherin (heart), and CDH13, is a unique member of the cadherin superfamily of proteins because it lacks the transmembrane and cytoplasmic domains common to all other cadherins and is instead anchored to the cell's plasma membrane by the GPI anchor.

<span class="mw-page-title-main">Cadherin-2</span>

Cadherin-2 also known as Neural cadherin (N-cadherin), is a protein that in humans is encoded by the CDH2 gene. CDH2 has also been designated as CD325 . Cadherin-2 is a transmembrane protein expressed in multiple tissues and functions to mediate cell–cell adhesion. In cardiac muscle, Cadherin-2 is an integral component in adherens junctions residing at intercalated discs, which function to mechanically and electrically couple adjacent cardiomyocytes. Alterations in expression and integrity of Cadherin-2 has been observed in various forms of disease, including human dilated cardiomyopathy. Variants in CDH2 have also been identified to cause a syndromic neurodevelopmental disorder.

<span class="mw-page-title-main">VE-cadherin</span> Protein-coding gene in the species Homo sapiens

Cadherin 5, type 2 or VE-cadherin also known as CD144, is a type of cadherin. It is encoded by the human gene CDH5.

<span class="mw-page-title-main">P120 (protein)</span> Protein-coding gene in the species Homo sapiens

p120, and called catenin delta-1 is a protein that in humans is encoded by the CTNND1 gene.

<span class="mw-page-title-main">IQGAP1</span>

Ras GTPase-activating-like protein IQGAP1 (IQGAP1) also known as p195 is a ubiquitously expressed protein that in humans is encoded by the IQGAP1 gene. IQGAP1 is a scaffold protein involved in regulating various cellular processes ranging from organization of the actin cytoskeleton, transcription, and cellular adhesion to regulating the cell cycle.

<span class="mw-page-title-main">Epithelial cell adhesion molecule</span> Transmembrane glycoprotein

Epithelial cell adhesion molecule (EpCAM), also known as CD326 among other names, is a transmembrane glycoprotein mediating Ca2+-independent homotypic cell–cell adhesion in epithelia. EpCAM is also involved in cell signaling, migration, proliferation, and differentiation. Additionally, EpCAM has oncogenic potential via its capacity to upregulate c-myc, e-fabp, and cyclins A & E. Since EpCAM is expressed exclusively in epithelia and epithelial-derived neoplasms, EpCAM can be used as diagnostic marker for various cancers. It appears to play a role in tumorigenesis and metastasis of carcinomas, so it can also act as a potential prognostic marker and as a potential target for immunotherapeutic strategies.

<span class="mw-page-title-main">PTPRM</span> Protein-coding gene in the species Homo sapiens

Receptor-type tyrosine-protein phosphatase mu is an enzyme that in humans is encoded by the PTPRM gene.

<span class="mw-page-title-main">CDH11</span> Protein-coding gene in the species Homo sapiens

Cadherin-11 is a protein that in humans is encoded by the CDH11 gene.

<span class="mw-page-title-main">CDH6</span> Protein-coding gene in the species Homo sapiens

Cadherin-6 is a protein that in humans is encoded by the CDH6 gene.

<span class="mw-page-title-main">CDH15</span> Protein-coding gene in the species Homo sapiens

Cadherin-15 is a protein that in humans is encoded by the CDH15 gene.

<span class="mw-page-title-main">CDH16</span> Protein-coding gene in the species Homo sapiens

Cadherin-16 is a protein that in humans is encoded by the CDH16 gene.

<span class="mw-page-title-main">CDH17</span> Protein-coding gene in the species Homo sapiens

Cadherin-17 is a protein that in humans is encoded by the CDH17 gene.

<span class="mw-page-title-main">CDH8</span> Protein-coding gene in the species Homo sapiens

Cadherin-8 is a protein that in humans is encoded by the CDH8 gene.

<span class="mw-page-title-main">Cadherin-1</span> Human protein-coding gene

Cadherin-1 or Epithelial cadherin(E-cadherin), is a protein that in humans is encoded by the CDH1 gene. Mutations are correlated with gastric, breast, colorectal, thyroid, and ovarian cancers. CDH1 has also been designated as CD324. It is a tumor suppressor gene.

<span class="mw-page-title-main">Catenin alpha-1</span> Protein-coding gene in the species Homo sapiens

αE-catenin, also known as Catenin alpha-1 is a protein that in humans is encoded by the CTNNA1 gene. αE-catenin is highly expressed in cardiac muscle and localizes to adherens junctions at intercalated disc structures where it functions to mediate the anchorage of actin filaments to the sarcolemma. αE-catenin also plays a role in tumor metastasis and skin cell function.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000062038 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000061048 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Kaupmann K, Becker-Follmann J, Scherer G, Jockusch H, Starzinski-Powitz A (Oct 1992). "The gene for the cell adhesion molecule M-cadherin maps to mouse chromosome 8 and human chromosome 16q24.1-qter and is near the E-cadherin (uvomorulin) locus in both species". Genomics. 14 (2): 488–90. doi:10.1016/S0888-7543(05)80247-2. PMID   1427864.
  6. 1 2 "Entrez Gene: CDH3 cadherin 3, type 1, P-cadherin (placental)".
  7. 1 2 3 4 Klingelhöfer J, Troyanovsky RB, Laur OY, Troyanovsky S (Aug 2000). "Amino-terminal domain of classic cadherins determines the specificity of the adhesive interactions". Journal of Cell Science. 113 (16): 2829–36. doi:10.1242/jcs.113.16.2829. PMID   10910767.
  8. 1 2 Schmeiser K, Grand RJ (Apr 1999). "The fate of E- and P-cadherin during the early stages of apoptosis". Cell Death and Differentiation. 6 (4): 377–86. doi: 10.1038/sj.cdd.4400504 . PMID   10381631.
  9. Lehtonen S, Lehtonen E, Kudlicka K, Holthöfer H, Farquhar MG (Sep 2004). "Nephrin forms a complex with adherens junction proteins and CASK in podocytes and in Madin-Darby canine kidney cells expressing nephrin". The American Journal of Pathology. 165 (3): 923–36. doi:10.1016/S0002-9440(10)63354-8. PMC   1618613 . PMID   15331416.
  10. Vieira AF, Paredes J (October 2015). "P-cadherin and the journey to cancer metastasis". Mol Cancer. 14: 178. doi:10.1186/s12943-015-0448-4. PMC   4595126 . PMID   26438065.
  11. Nose A, Takeichi M (December 1986). "A novel cadherin cell adhesion molecule: its expression patterns associated with implantation and organogenesis of mouse embryos". J Cell Biol. 103 (6 Pt 2): 2649–58. doi:10.1083/jcb.103.6.2649. PMC   2114609 . PMID   3539943.

Further reading