Epiplakin
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.[7] The domains in epiplakin range from 46-70% in their homology to this B domain in desmoplakin.[8] 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]
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 epthelial 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]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000261150 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b c d 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.
- ^ 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.
- ^ "Entrez Gene: EPPK1 epiplakin 1".
- ^ 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.
- ^ 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.
- ^ 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.
- ^ a b 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.
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Further reading
- Fujiwara S, Kohno K, Iwamatsu A, Naito I, Shinkai H (May 1996). "Identification of a 450-kDa human epidermal autoantigen as a new member of the plectin family". The Journal of Investigative Dermatology. 106 (5): 1125–30. doi:10.1111/1523-1747.ep12340171. PMID 8618051.
- Blagoev B, Kratchmarova I, Ong SE, Nielsen M, Foster LJ, Mann M (March 2003). "A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling". Nature Biotechnology. 21 (3): 315–8. doi:10.1038/nbt790. PMID 12577067.
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
- Spazierer D, Fuchs P, Pröll V, Janda L, Oehler S, Fischer I, et al. (August 2003). "Epiplakin gene analysis in mouse reveals a single exon encoding a 725-kDa protein with expression restricted to epithelial tissues". The Journal of Biological Chemistry. 278 (34): 31657–66. doi:10.1074/jbc.M303055200. PMID 12791695.
- 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.
- Kim JE, Tannenbaum SR, White FM (2005). "Global phosphoproteome of HT-29 human colon adenocarcinoma cells". Journal of Proteome Research. 4 (4): 1339–46. doi:10.1021/pr050048h. PMID 16083285.
- Nousiainen M, Silljé HH, Sauer G, Nigg EA, Körner R (April 2006). "Phosphoproteome analysis of the human mitotic spindle". Proceedings of the National Academy of Sciences of the United States of America. 103 (14): 5391–6. Bibcode:2006PNAS..103.5391N. doi:10.1073/pnas.0507066103. PMC 1459365. PMID 16565220.
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
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