Desmoplakin

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Desmoplakin
Protein DSP PDB 1lm5.png
PDB rendering based on 1lm5.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols DSP ; DP; DPI; DPII
External IDs OMIM125647 MGI109611 HomoloGene37922 GeneCards: DSP Gene
RNA expression pattern
PBB GE DSP 200606 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1832 109620
Ensembl ENSG00000096696 ENSMUSG00000054889
UniProt P15924 E9Q557
RefSeq (mRNA) NM_001008844 NM_023842
RefSeq (protein) NP_001008844 NP_076331
Location (UCSC) Chr 6:
7.54 – 7.59 Mb
Chr 13:
38.15 – 38.2 Mb
PubMed search [1] [2]
Cell adhesion in desmosomes

Desmoplakin is a protein associated with desmosomes.[1]

Desmoplakin is a protein in humans that is encoded by the DSP gene.[2][3]

Desmosomes are intercellular junctions that tightly link adjacent cells. Desmoplakin is an obligate component of functional desmosomes that anchors intermediate filaments to desmosomal plaques. The N-terminus of desmoplakin is required for localization to the desmosome and interacts with the N-terminal region of plakophilin 1 and plakoglobin. This is further sub divided into a region called the "Plakin domain" made up of repetitive domains called Spectrin repeats. A crystal structure of part of the plakin domain has been resolved,[4] while the entire plakin domain has been elucidated using Small angle X-ray scattering which revealed a non-linear structure, an unexpected result considering spectrin repeats are observed in linear orientations.[5] The C-terminus of desmoplakin binds with intermediate filaments. These are further sub divided to three homologous Plakin repeat domains (see PDBs below). In the mid-region of desmoplakin, a coiled-coiled rod domain is responsible for homodimerization. Mutations in this gene are the cause of several cardiomyopathies and keratodermas as well as the autoimmune disease paraneoplastic pemphigus.[3]

Interactions[edit]

Desmoplakin has been shown to interact with Plakoglobin,[6][7] Vimentin,[8] Keratin 1,[8] Desmin,[8] PKP1[9] and PKP2.[10]

See also[edit]

References[edit]

  1. ^ Bornslaeger EA, Corcoran CM, Stappenbeck TS, Green KJ (August 1996). "Breaking the connection: displacement of the desmosomal plaque protein desmoplakin from cell-cell interfaces disrupts anchorage of intermediate filament bundles and alters intercellular junction assembly". J. Cell Biol. 134 (4): 985–1001. doi:10.1083/jcb.134.4.985. PMC 2120955. PMID 8769422. 
  2. ^ Arnemann J, Spurr NK, Wheeler GN, Parker AE, Buxton RS (October 1991). "Chromosomal assignment of the human genes coding for the major proteins of the desmosome junction, desmoglein DGI (DSG), desmocollins DGII/III (DSC), desmoplakins DPI/II (DSP), and plakoglobin DPIII (JUP)". Genomics 10 (3): 640–5. doi:10.1016/0888-7543(91)90446-L. PMID 1889810. 
  3. ^ a b "Entrez Gene: DSP desmoplakin". 
  4. ^ Choi, HJ; Weis, WI (2011). "Crystal structure of a rigid four-spectrin-repeat fragment of the human desmoplakin plakin domain.". Journal of Molecular Biology 409 (5): 800–12. doi:10.1016/j.jmb.2011.04.046. PMC 3107870. PMID 21536047. 
  5. ^ Al-Jassar, C; Knowles, T; Jeeves, M; Kami, K; Behr, E; Bikker, H; Overduin, M; Chidgey, M (2011). "The Nonlinear Structure of the Desmoplakin Plakin Domain and the Effects of Cardiomyopathy-Linked Mutations.". Journal of Molecular Biology 411 (5): 1049–61. doi:10.1016/j.jmb.2011.06.047. PMID 21756917. 
  6. ^ Kowalczyk, A P; Navarro P; Dejana E; Bornslaeger E A; Green K J; Kopp D S; Borgwardt J E (October 1998). "VE-cadherin and desmoplakin are assembled into dermal microvascular endothelial intercellular junctions: a pivotal role for plakoglobin in the recruitment of desmoplakin to intercellular junctions". J. Cell. Sci. (ENGLAND) 111 (20): 3045–57. ISSN 0021-9533. PMID 9739078. 
  7. ^ Kowalczyk, A P; Bornslaeger E A; Borgwardt J E; Palka H L; Dhaliwal A S; Corcoran C M; Denning M F; Green K J (November 1997). "The amino-terminal domain of desmoplakin binds to plakoglobin and clusters desmosomal cadherin-plakoglobin complexes". J. Cell Biol. (UNITED STATES) 139 (3): 773–84. doi:10.1083/jcb.139.3.773. ISSN 0021-9525. PMC 2141713. PMID 9348293. 
  8. ^ a b c Meng, J J; Bornslaeger E A; Green K J; Steinert P M; Ip W (August 1997). "Two-hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type-specific intermediate filaments". J. Biol. Chem. (UNITED STATES) 272 (34): 21495–503. doi:10.1074/jbc.272.34.21495. ISSN 0021-9258. PMID 9261168. 
  9. ^ Hofmann, I; Mertens C; Brettel M; Nimmrich V; Schnölzer M; Herrmann H (July 2000). "Interaction of plakophilins with desmoplakin and intermediate filament proteins: an in vitro analysis". J. Cell. Sci. (ENGLAND) 113 (13): 2471–83. ISSN 0021-9533. PMID 10852826. 
  10. ^ Chen, Xinyu; Bonne Stefan; Hatzfeld Mechthild; van Roy Frans; Green Kathleen J (March 2002). "Protein binding and functional characterization of plakophilin 2. Evidence for its diverse roles in desmosomes and beta -catenin signaling". J. Biol. Chem. (United States) 277 (12): 10512–22. doi:10.1074/jbc.M108765200. ISSN 0021-9258. PMID 11790773. 

Further reading[edit]

External links[edit]