Plakophilin 3 – a novel cell-type-specific desmosomal plaque protein

Schmidt, Ansgar; Langbein, Lutz; Prätzel, Silke; Rode, Michaela; Rackwitz, Hans Richard; Franke, Werner W.

doi:10.1046/j.1432-0436.1999.6450291.x

Cited by 66 publications

(107 citation statements)

References 68 publications

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“…Within the amino-terminal head domain, plakophilins share a region of high homology called the HR2 domain, which can be further divided into two smaller segments separated by a linker of poorly conserved sequence (12). Presently, the function of the HR2 domain is unknown.…”

Section: The Carboxyl Terminus Of Plakophilin-1 Is Required For Itsmentioning

confidence: 99%

Carboxyl Terminus of Plakophilin-1 Recruits It to Plasma Membrane, whereas Amino Terminus Recruits Desmoplakin and Promotes Desmosome Assembly

Sobolik-Delmaire

Katafiasz

Wahl

2006

Journal of Biological Chemistry

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Plakophilins are armadillo repeat-containing proteins, initially identified as desmosomal plaque proteins that have subsequently been shown to also localize to the nucleus. Loss of plakophilin-1 is the underlying cause of ectodermal dysplasia/skin fragility syndrome, and skin from these patients exhibits desmosomes that are reduced in size and number. Thus, it has been suggested that plakophilin-1 plays an important role in desmosome stability and/or assembly. In this study, we used a cell culture system (A431DE cells) that expresses all of the proteins necessary to assemble a desmosome, except plakophilin-1. Using this cell line, we sought to determine the role of plakophilin-1 in de novo desmosome assembly. When exogenous plakophilin-1 was expressed in these cells, desmosomes were assembled, as assessed by electron microscopy and immunofluorescence localization of desmoplakin, into punctate structures. Deletion mutagenesis experiments revealed that amino acids 686 -726 in the carboxyl terminus of plakophilin-1 are required for its localization to the plasma membrane. In addition, we showed that amino acids 1-34 in the amino terminus were necessary for subsequent recruitment of desmoplakin to the membrane and desmosome assembly.

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Section: The Carboxyl Terminus Of Plakophilin-1 Is Required For Itsmentioning

confidence: 99%

Carboxyl Terminus of Plakophilin-1 Recruits It to Plasma Membrane, whereas Amino Terminus Recruits Desmoplakin and Promotes Desmosome Assembly

Sobolik-Delmaire

Katafiasz

Wahl

2006

Journal of Biological Chemistry

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“…1,2 They consist of the transmembrane cell adhesion proteins, the desmogleins (DSG) and desmocollins (DSC), members of the cadherin superfamily, and the constitutive cytoplasmic plaque proteins, desmoplakin and plakoglobin and various accessory proteins such as plakophilins 1, 2 and 3 3 which are involved in the linkage with the intermediate filaments.…”

Section: Introductionmentioning

confidence: 99%

Spectrum of dominant mutations in the desmosomal cadherin desmoglein 1, causing the skin disease striate palmoplantar keratoderma

Hunt¹,

Rickman²,

Whittock

et al. 2001

Eur J Hum Genet

108

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The adhesive proteins of the desmosome type of cell junction consist of two types of cadherin found exclusively in that structure, the desmogleins and desmocollins, coded by two closely linked loci on human chromosome 18q12.1. Recently we have identified a mutation in the DSG1 gene coding for desmoglein 1 as the cause of the autosomal dominant skin disease striate palmoplantar keratoderma (SPPK) in which affected individuals have marked hyperkeratotic bands on the palms and soles. In the present study we present the complete exon-intron structure of the DSG1 gene, which occupies approximately 43 kb, and intron primers sufficient to amplify all the exons. Using these we have analysed the mutational changes in this gene in five further cases of SPPK. All were heterozygotic mutations in the extracellular domain leading to a truncated protein, due either to an addition or deletion of a single base, or a base change resulting in a stop codon. Three mutations were in exon 9 and one in exon 11, both of which code for part of the third and fourth extracellular domains, and one was in exon 2 coding for part of the prosequence of this processed protein. This latter mutation thus results in the mutant allele synthesising only 25 amino acid residues of the prosequence of the protein so that this is effectively a null mutation implying that dominance in the case of this mutation was caused by haploinsufficiency. The most severe consequences of SPPK mutations are in regions of the body where pressure and abrasion are greatest and where desmosome function is most necessary. SPPK therefore provides a very sensitive measure of desmosomal function.

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“…The obvious example is the staining pattern for ␤-catenin where, in postimplantation embryos, it clearly localizes to more nuclei in EE cells at the primitive streak than nuclei of surrounding nonprimitive streak EE cells (Mohamed et al, 2004). Conversely, arm proteins such as plakophilins, show a broader nuclear staining pattern and, correspondingly, do not appear to have a nuclear function early in development (i.e., fertilization-E7.5; Schmidt et al, 1999;South et al, 2003;Grossmann et al, 2004).…”

Section: Fig 12 A-fmentioning

confidence: 99%

Dynamics and unexpected localization of the plakin binding protein, kazrin, in mouse eggs and early embryos

Gallicano

Foshay

Pengetnze

et al. 2005

Developmental Dynamics

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The cell uses the cytoskeleton in virtually every aspect of cell survival and function. One primary function of the cytoskeleton is to connect to and stabilize intercellular junctions. To accomplish this task, microtubules, actin filaments, and intermediate filaments utilize cytolinker proteins, which physically bind the cytoskeletal filament to the core proteins of the adhesion junction. The plakin family of linker proteins have been in the spotlight recently as critical components for embryo survival and, when mutated, the cause of diseases such as muscular dystrophy and cardiomyopathies. Here, we reveal the dynamics of a recently discovered plakin binding protein, kazrin (kaz), during early mouse development. Kaz was originally found in adult tissues, primarily epidermis, linking periplakin to the plasma membrane and colocalizing with desmoplakin in desmosomes. Using reverse transcriptase-polymerase chain reaction, Western blots, and confocal microscopy, we found kaz in unfertilized eggs associated with the spindle apparatus and cytoskeletal sheets. As quickly as 5 min after egg activation, kaz relocates to a diffuse peri-spindle position, followed 20 -30 min later by clear localization to the presumptive cytokinetic ring. Before the blastocyst stage of development, kaz associates with the nuclear matrix in a cell cycle-dependent manner, and also associates with the cytoplasmic actin cytoskeleton. After blastocyst formation, kaz localization and potential function(s) become highly complex as it is found associating with cell-cell junctions, the cytoskeleton, and nucleus. Postimplantation stages of development reveal that kaz retains a multifunctional, tissue-specific role as it is detected at diverse locations in various embryonic tissue types.

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Plakophilin 3 – a novel cell-type-specific desmosomal plaque protein

Cited by 66 publications

References 68 publications

Carboxyl Terminus of Plakophilin-1 Recruits It to Plasma Membrane, whereas Amino Terminus Recruits Desmoplakin and Promotes Desmosome Assembly

Carboxyl Terminus of Plakophilin-1 Recruits It to Plasma Membrane, whereas Amino Terminus Recruits Desmoplakin and Promotes Desmosome Assembly

Spectrum of dominant mutations in the desmosomal cadherin desmoglein 1, causing the skin disease striate palmoplantar keratoderma

Dynamics and unexpected localization of the plakin binding protein, kazrin, in mouse eggs and early embryos

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