PKP2

PKP2

Plakophilin 2, also known as PKP2, is a human gene.cite web | title = Entrez Gene: PKP2 plakophilin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5318| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene encodes a member of the arm-repeat (armadillo) and plakophilin gene families. Plakophilin proteins contain numerous armadillo repeats, localize to cell desmosomes and nuclei, and participate in linking cadherins to intermediate filaments in the cytoskeleton. This gene product may regulate the signaling activity of beta-catenin. Two alternately spliced transcripts encoding two protein isoforms have been identified. A processed pseudogene with high similarity to this locus has been mapped to chromosome 12p13.cite web | title = Entrez Gene: PKP2 plakophilin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5318| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Mertens C, Kuhn C, Franke WW |title=Plakophilins 2a and 2b: constitutive proteins of dual location in the karyoplasm and the desmosomal plaque. |journal=J. Cell Biol. |volume=135 |issue= 4 |pages= 1009–25 |year= 1997 |pmid= 8922383 |doi=
*cite journal | author=Bonné S, van Hengel J, van Roy F |title=Chromosomal mapping of human armadillo genes belonging to the p120(ctn)/plakophilin subfamily. |journal=Genomics |volume=51 |issue= 3 |pages= 452–4 |year= 1998 |pmid= 9721216 |doi= 10.1006/geno.1998.5398
*cite journal | author=Mertens C, Kuhn C, Moll R, "et al." |title=Desmosomal plakophilin 2 as a differentiation marker in normal and malignant tissues. |journal=Differentiation |volume=64 |issue= 5 |pages= 277–90 |year= 1999 |pmid= 10374264 |doi=
*cite journal | author=Schmidt A, Langbein L, Prätzel S, "et al." |title=Plakophilin 3--a novel cell-type-specific desmosomal plaque protein. |journal=Differentiation |volume=64 |issue= 5 |pages= 291–306 |year= 1999 |pmid= 10374265 |doi=
*cite journal | author=Bonné S, van Hengel J, van Roy F |title=Assignment of the plakophilin-2 gene (PKP2) and a plakophilin-2 pseudogene (PKP2P1) to human chromosome bands 12p11 and 12p13, respectively, by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=88 |issue= 3-4 |pages= 286–7 |year= 2000 |pmid= 10828611 |doi=
*cite journal | author=Hofmann I, Mertens C, Brettel M, "et al." |title=Interaction of plakophilins with desmoplakin and intermediate filament proteins: an in vitro analysis. |journal=J. Cell. Sci. |volume=113 ( Pt 13) |issue= |pages= 2471–83 |year= 2000 |pmid= 10852826 |doi=
*cite journal | author=Mertens C, Hofmann I, Wang Z, "et al." |title=Nuclear particles containing RNA polymerase III complexes associated with the junctional plaque protein plakophilin 2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 14 |pages= 7795–800 |year= 2001 |pmid= 11416169 |doi= 10.1073/pnas.141219498
*cite journal | author=Chen X, Bonne S, Hatzfeld M, "et al." |title=Protein binding and functional characterization of plakophilin 2. Evidence for its diverse roles in desmosomes and beta -catenin signaling. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10512–22 |year= 2002 |pmid= 11790773 |doi= 10.1074/jbc.M108765200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Müller J, Ritt DA, Copeland TD, Morrison DK |title=Functional analysis of C-TAK1 substrate binding and identification of PKP2 as a new C-TAK1 substrate. |journal=EMBO J. |volume=22 |issue= 17 |pages= 4431–42 |year= 2003 |pmid= 12941695 |doi= 10.1093/emboj/cdg426
*cite journal | author=Colland F, Jacq X, Trouplin V, "et al." |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324–32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104
*cite journal | author=Jin J, Smith FD, Stark C, "et al." |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436–50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051
*cite journal | author=Gerull B, Heuser A, Wichter T, "et al." |title=Mutations in the desmosomal protein plakophilin-2 are common in arrhythmogenic right ventricular cardiomyopathy. |journal=Nat. Genet. |volume=36 |issue= 11 |pages= 1162–4 |year= 2004 |pmid= 15489853 |doi= 10.1038/ng1461
*cite journal | author=Benzinger A, Muster N, Koch HB, "et al." |title=Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer. |journal=Mol. Cell Proteomics |volume=4 |issue= 6 |pages= 785–95 |year= 2005 |pmid= 15778465 |doi= 10.1074/mcp.M500021-MCP200
*cite journal | author=Kimura K, Wakamatsu A, Suzuki Y, "et al." |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406
*cite journal | author=Syrris P, Ward D, Asimaki A, "et al." |title=Clinical expression of plakophilin-2 mutations in familial arrhythmogenic right ventricular cardiomyopathy. |journal=Circulation |volume=113 |issue= 3 |pages= 356–64 |year= 2006 |pmid= 16415378 |doi= 10.1161/CIRCULATIONAHA.105.561654
*cite journal | author=Dalal D, Molin LH, Piccini J, "et al." |title=Clinical features of arrhythmogenic right ventricular dysplasia/cardiomyopathy associated with mutations in plakophilin-2. |journal=Circulation |volume=113 |issue= 13 |pages= 1641–9 |year= 2006 |pmid= 16549640 |doi= 10.1161/CIRCULATIONAHA.105.568642
*cite journal | author=van Tintelen JP, Entius MM, Bhuiyan ZA, "et al." |title=Plakophilin-2 mutations are the major determinant of familial arrhythmogenic right ventricular dysplasia/cardiomyopathy. |journal=Circulation |volume=113 |issue= 13 |pages= 1650–8 |year= 2006 |pmid= 16567567 |doi= 10.1161/CIRCULATIONAHA.105.609719
*cite journal | author=Kannankeril PJ, Bhuiyan ZA, Darbar D, "et al." |title=Arrhythmogenic right ventricular cardiomyopathy due to a novel plakophilin 2 mutation: wide spectrum of disease in mutation carriers within a family. |journal=Heart rhythm : the official journal of the Heart Rhythm Society |volume=3 |issue= 8 |pages= 939–44 |year= 2007 |pmid= 16876743 |doi= 10.1016/j.hrthm.2006.04.028
*cite journal | author=Dalal D, James C, Devanagondi R, "et al." |title=Penetrance of mutations in plakophilin-2 among families with arrhythmogenic right ventricular dysplasia/cardiomyopathy. |journal=J. Am. Coll. Cardiol. |volume=48 |issue= 7 |pages= 1416–24 |year= 2006 |pmid= 17010805 |doi= 10.1016/j.jacc.2006.06.045

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Нужна курсовая?

Look at other dictionaries:

  • Desmoplakin — PDB rendering based on 1lm5 …   Wikipedia

  • Microtubule — Space filling model of a microtubule segment derived from cryo electron microscopy. The protofilaments are seen running along the axis of the segment. The microtubule (+) end is towards the top of the image.[1] Microtubules are a component of the …   Wikipedia

  • Keratin — Not to be confused with kerogen, carotene, chitin, or creatine. Microscopy of keratin filaments inside cells. Keratin refers to a family of fibrous structural proteins. Keratin is the key structural material making up the outer layer of human… …   Wikipedia

  • Cytoskeleton — The eukaryotic cytoskeleton. Actin filaments are shown in red, microtubules in green, and the nuclei are in blue. The cytoskeleton (also CSK) is a cellular scaffolding or skeleton contained within a cell s cytoplasm and is made out of protein.… …   Wikipedia

  • Microfilament — Actin cytoskeleton of mouse embryo fibroblasts, stained with Fluorescein isothiocyanate phalloidin Microfilaments ( or actin filaments) are the thinnest filaments of the cytoskeleton, a structure found in the cytoplasm of all eukaryotic cells.… …   Wikipedia

  • Actin — G Actin (PDB code: 1j6z). ADP and the divalent cation are highlighted …   Wikipedia

  • Myosin — Part of the myosin II structure. Atoms in the heavy chain are colored red on the left hand side, and atoms in the light chains are colored orange and yellow. Myosins comprise a family of ATP dependent motor proteins and are best known for their… …   Wikipedia

  • Lamin — Nuclear lamins, also known as Class V intermediate filaments, are fibrous proteins providing structural function and transcriptional regulation in the cell nucleus. Nuclear lamins interact with membrane associated proteins to form the nuclear… …   Wikipedia

  • MreB — Procaryotic MreB (PDB code: 1jce) in cartoon representation. The fold of the protein is similar to its eukaryotic counterpart actin. MreB is a protein found in bacteria that has been identified as a homologue of actin, as indicated by… …   Wikipedia

  • Arrhythmogenic right ventricular dysplasia — Classification and external resources Photomicrograph of an ARVC heart. ICD 10 I …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”