Epiplakin

Last updated
EPPK1
Identifiers
Aliases EPPK1 , EPIPL, EPIPL1, epiplakin 1
External IDs OMIM: 607553 MGI: 2386306 HomoloGene: 20006 GeneCards: EPPK1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_031308

NM_144848

RefSeq (protein)

NP_112598

NP_659097

Location (UCSC) Chr 8: 143.86 – 143.88 Mb n/a
PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Epiplakin is a protein that in humans is encoded by the EPPK1 gene. [4] [5] [6] It belongs to the family of plakin proteins and is found in the human epidermis. [4] It consists of 13 domains which are all similar to the B domain located at the C terminus of the human epidermal and cardiac muscle protein desmoplakin. [4] The domains in epiplakin range from 46 to 70% in their homology to this B domain in desmoplakin. [7] It was first identified as an autoantigen in a person who suffers from a rare autoimmune skin disease. [4] Epiplakin was sequenced to have a total of 5065 amino acid residues and based on its amino acid composition it has a molecular weight of about 552 kDa. [4] The EPPK1 gene is notable for a lack of introns over its coding region - its entire 15 kbp coding region is encoded by a single exon. [8]

Epiplakin has been found to bind to keratin filaments and may contribute to inhibiting the growth of the filaments. This is suspected due to keratin bound epiplakin being found primarily at branch-points and end-points of the keratin filaments. [9] Blocking the expression of epiplakin in cultured corneal epithelial cells via siRNA has been associated with faster wound closure and faster migration of corneal cells. [10] This may be due to the loss of epiplakin leading to a modification of the cytoskeleton in epithelial cells. [10]

Related Research Articles

<span class="mw-page-title-main">Keratin</span> One of a family of fibrous structural proteins

Keratin is one of a family of structural fibrous proteins also known as scleroproteins. Alpha-keratin (α-keratin) is a type of keratin found in vertebrates. It is the key structural material making up scales, hair, nails, feathers, horns, claws, hooves, and the outer layer of skin among vertebrates. Keratin also protects epithelial cells from damage or stress. Keratin is extremely insoluble in water and organic solvents. Keratin monomers assemble into bundles to form intermediate filaments, which are tough and form strong unmineralized epidermal appendages found in reptiles, birds, amphibians, and mammals. Excessive keratinization participate in fortification of certain tissues such as in horns of cattle and rhinos, and armadillos' osteoderm. The only other biological matter known to approximate the toughness of keratinized tissue is chitin. Keratin comes in two types, the primitive, softer forms found in all vertebrates and harder, derived forms found only among sauropsids.

<span class="mw-page-title-main">Desmosome</span> Cell junction involved in cell-to-cell adhesion

A desmosome, also known as a macula adherens, is a cell structure specialized for cell-to-cell adhesion. A type of junctional complex, they are localized spot-like adhesions randomly arranged on the lateral sides of plasma membranes. Desmosomes are one of the stronger cell-to-cell adhesion types and are found in tissue that experience intense mechanical stress, such as cardiac muscle tissue, bladder tissue, gastrointestinal mucosa, and epithelia.

<span class="mw-page-title-main">Keratin 1</span>

Keratin 1 is a Type II intermediate filament (IFs) of the intracytoplasmatic cytoskeleton. Is co-expressed with and binds to Keratin 10, a Type I keratin, to form a coiled coil heterotypic keratin chain. Keratin 1 and Keratin 10 are specifically expressed in the spinous and granular layers of the epidermis. In contrast, basal layer keratinocytes express little to no Keratin 1. Mutations in KRT1, the gene encoding Keratin 1, have been associated with variants of the disease bullous congenital ichthyosiform erythroderma in which the palms and soles of the feet are affected. Mutations in KRT10 have also been associated with bullous congenital ichthyosiform erythroderma; however, in patients with KRT10 mutations the palms and soles are spared. This difference is likely due to Keratin 9, rather than Keratin 10, being the major binding partner of Keratin 1 in acral keratinocytes.

<span class="mw-page-title-main">Keratin 7</span>

Keratin, type II cytoskeletal 7 also known as cytokeratin-7 (CK-7) or keratin-7 (K7) or sarcolectin (SCL) is a protein that in humans is encoded by the KRT7 gene. Keratin 7 is a type II keratin. It is specifically expressed in the simple epithelia lining the cavities of the internal organs and in the gland ducts and blood vessels.

<span class="mw-page-title-main">Keratin 14</span> Protein-coding gene in the species Homo sapiens

Keratin 14 is a member of the type I keratin family of intermediate filament proteins. Keratin 14 was the first type I keratin sequence determined. Keratin 14 is also known as cytokeratin-14 (CK-14) or keratin-14 (KRT14). In humans it is encoded by the KRT14 gene.

<span class="mw-page-title-main">Keratin 19</span> Protein-coding gene in the species Homo sapiens

Keratin, type I cytoskeletal 19 also known as cytokeratin-19 (CK-19) or keratin-19 (K19) is a 40 kDa protein that in humans is encoded by the KRT19 gene. Keratin 19 is a type I keratin.

<span class="mw-page-title-main">Keratin 18</span>

Keratin 18 is a type I cytokeratin. It is, together with its filament partner keratin 8, perhaps the most commonly found products of the intermediate filament gene family. They are expressed in single layer epithelial tissues of the body. Mutations in this gene have been linked to cryptogenic cirrhosis. Two transcript variants encoding the same protein have been found for this gene.

<span class="mw-page-title-main">Keratin 15</span> Protein-coding gene in the species Homo sapiens

Keratin 15 is a protein that in humans is encoded by the KRT15 gene. It has also been referred to as cytokeratin 15, K1CO and KRTB.

Hair keratin is a type of keratin found in hair and the nails.

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

Hemidesmosomes are very small stud-like structures found in keratinocytes of the epidermis of skin that attach to the extracellular matrix. They are similar in form to desmosomes when visualized by electron microscopy, however, desmosomes attach to adjacent cells. Hemidesmosomes are also comparable to focal adhesions, as they both attach cells to the extracellular matrix. Instead of desmogleins and desmocollins in the extracellular space, hemidesmosomes utilize integrins. Hemidesmosomes are found in epithelial cells connecting the basal epithelial cells to the lamina lucida, which is part of the basal lamina. Hemidesmosomes are also involved in signaling pathways, such as keratinocyte migration or carcinoma cell intrusion.

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

Filaggrin is a filament-associated protein that binds to keratin fibers in epithelial cells. Ten to twelve filaggrin units are post-translationally hydrolyzed from a large profilaggrin precursor protein during terminal differentiation of epidermal cells. In humans, profilaggrin is encoded by the FLG gene, which is part of the S100 fused-type protein (SFTP) family within the epidermal differentiation complex on chromosome 1q21.

<span class="mw-page-title-main">Desmoglein-1</span> Protein found in humans

Desmoglein-1 is a protein that in humans is encoded by the DSG1 gene. Desmoglein-1 is expressed everywhere in the skin epidermis, but mainly it is expressed in the superficial upper layers of the skin epidermis.

<span class="mw-page-title-main">Desmoplakin</span> Protein found in humans

Desmoplakin is a protein in humans that is encoded by the DSP gene. Desmoplakin is a critical component of desmosome structures in cardiac muscle and epidermal cells, which function to maintain the structural integrity at adjacent cell contacts. In cardiac muscle, desmoplakin is localized to intercalated discs which mechanically couple cardiac cells to function in a coordinated syncytial structure. Mutations in desmoplakin have been shown to play a role in dilated cardiomyopathy and arrhythmogenic right ventricular cardiomyopathy, where it may present with acute myocardial injury; striate palmoplantar keratoderma, Carvajal syndrome and paraneoplastic pemphigus.

<span class="mw-page-title-main">Keratin 8</span>

Keratin, type II cytoskeletal 8 also known as cytokeratin-8 (CK-8) or keratin-8 (K8) is a keratin protein that is encoded in humans by the KRT8 gene. It is often paired with keratin 18.

<span class="mw-page-title-main">Keratin 5</span>

Keratin 5, also known as KRT5, K5, or CK5, is a protein that is encoded in humans by the KRT5 gene. It dimerizes with keratin 14 and forms the intermediate filaments (IF) that make up the cytoskeleton of basal epithelial cells. This protein is involved in several diseases including epidermolysis bullosa simplex and breast and lung cancers.

<span class="mw-page-title-main">Collagen, type XVII, alpha 1</span> Mammalian protein found in humans

Collagen XVII, previously called BP180, is a transmembrane protein which plays a critical role in maintaining the linkage between the intracellular and the extracellular structural elements involved in epidermal adhesion, identified by Diaz and colleagues in 1990.

<span class="mw-page-title-main">Dystonin</span> Neurologically significant human protein

Dystonin(DST), also known as bullous pemphigoid antigen 1 (BPAG1), isoforms 1/2/3/4/5/8, is a protein that in humans is encoded by the DST gene.

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

Periplakin is a protein that in humans is encoded by the PPL gene.

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

Envoplakin is a protein that in humans is encoded by the EVPL gene.

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

Trichohyalin is a protein that in mammals is encoded by the TCHH gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000261150 - Ensembl, May 2017
  2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. 1 2 3 4 5 Fujiwara S, Takeo N, Otani Y, Parry DA, Kunimatsu M, Lu R, et al. (April 2001). "Epiplakin, a novel member of the Plakin family originally identified as a 450-kDa human epidermal autoantigen. Structure and tissue localization". The Journal of Biological Chemistry. 276 (16): 13340–7. doi: 10.1074/jbc.M011386200 . PMID   11278896.
  5. Jang SI, Kalinin A, Takahashi K, Marekov LN, Steinert PM (February 2005). "Characterization of human epiplakin: RNAi-mediated epiplakin depletion leads to the disruption of keratin and vimentin IF networks". Journal of Cell Science. 118 (Pt 4): 781–93. doi:10.1242/jcs.01647. PMID   15671067. S2CID   38183338.
  6. "Entrez Gene: EPPK1 epiplakin 1".
  7. Takeo N, Wang W, Matsuo N, Sumiyoshi H, Yoshioka H, Fujiwara S (November 2003). "Structure and heterogeneity of the human gene for epiplakin (EPPK1)". The Journal of Investigative Dermatology. 121 (5): 1224–6. doi: 10.1046/j.1523-1747.2003.12550_5.x . PMID   14708632.
  8. Stewart S (2008). A short guide to the human genome. Cold Spring Harbor Laboratory Press. ISBN   978-0-87969-791-4. OCLC   301791139.
  9. Wang W, Sumiyoshi H, Yoshioka H, Fujiwara S (August 2006). "Interactions between epiplakin and intermediate filaments". The Journal of Dermatology. 33 (8): 518–27. doi:10.1111/j.1346-8138.2006.00127.x. PMID   16923132. S2CID   25372989.
  10. 1 2 Kokado M, Okada Y, Miyamoto T, Yamanaka O, Saika S (May 2016). "Effects of epiplakin-knockdown in cultured corneal epithelial cells". BMC Research Notes. 9 (1): 278. doi: 10.1186/s13104-016-2082-7 . PMC   4873999 . PMID   27206504.

Further reading