The N Terminus of the Transmembrane Protein BP180 Interacts with the N-terminal Domain of BP230, Thereby Mediating Keratin Cytoskeleton Anchorage to the Cell Surface at the Site of the Hemidesmosome

Hopkinson, Susan B.; Jones, Jonathan

doi:10.1091/mbc.11.1.277

Cited by 106 publications

(96 citation statements)

References 39 publications

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“…Epidermal BPAG1e interacts with the hemidesmosomal proteins α6β4 integrin and collagen XVII in basal keratinocytes and mediates epidermal-dermal cohesion (Borradori and Sonnenberg, 1999;Hopkinson and Jones, 2000;Koster et al, 2003;Leung et al, 2001b;Litjens et al, 2006;Sawamura et al, 1991a,b). In addition, BPAG1e also binds to the epidermal cytokeratin network that is formed by keratins 5 and 14 (K5, K14) in basal keratinocytes and thereby connects them to the extracellular matrix (Fontao et al, 2003;Guo et al, 1995).…”

Section: Cellular Functions Of Bpag1mentioning

confidence: 99%

Spectraplakin family proteins – cytoskeletal crosslinkers with versatile roles

Zhang

Yue

2017

Journal of Cell Science

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The different cytoskeletal networks in a cell are responsible for many fundamental cellular processes. Current studies have shown that spectraplakins, cytoskeletal crosslinkers that combine features of both the spectrin and plakin families of crosslinkers, have a critical role in integrating these different cytoskeletal networks. Spectraplakin genes give rise to a variety of isoforms that have distinct functions. Importantly, all spectraplakin isoforms are uniquely able to associate with all three elements of the cytoskeleton, namely, F-actin, microtubules and intermediate filaments. In this Review, we will highlight recent studies that have unraveled their function in a wide range of different processes, from regulating cell adhesion in skin keratinocytes to neuronal cell migration. Taken together, this work has revealed a diverse and indispensable role for orchestrating the function of different cytoskeletal elements in vivo.

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Section: Cellular Functions Of Bpag1mentioning

confidence: 99%

Spectraplakin family proteins – cytoskeletal crosslinkers with versatile roles

Zhang

Yue

2017

Journal of Cell Science

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“…In the case of the epithelial dystonin-e protein, this most certainly appears to be the case. Dystonin-e plays a wellestablished role of linking keratin intermediate filaments to hemi-desmosomes within keratinocytes [Hopkinson and Jones, 2000]. In the nervous system, no hemidesmosomes or keratin filaments are present, and the domain structure of the major neuronal dystonin (dystonina) isoforms differs greatly from the epithelial isoform (Fig.…”

Section: Dystonin Is Essential To Neurons-but For What?mentioning

confidence: 99%

“…This protein was predicted to be involved in tethering intermediate filaments at the site of hemidesmosomes in the keratinocyte cells of the skin [Sawamura et al, 1991], a prediction later confirmed [Hopkinson and Jones, 2000]. It may be the case that a disruption in the tethering function of BPAG1 results in a breakdown in the mechanical linkage between keratinocytes and the underlying basement membrane.…”

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confidence: 99%

Dystonin/Bpag1—A link to what?

Young

Kothary

2007

Cell Motil. Cytoskeleton

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The dystonin/Bpag1 cytoskeletal interacting proteins play important roles in maintaining cytoarchitecture integrity in skin and in the neuromuscular system. The most profound phenotype observed in the dystonin mutant dystonia musculorum (dt) mice is a severe movement disorder, attributed in large part to sensory neuron degeneration. The molecular basis for this phenotype is currently not clear, despite several studies indicating possible causes for the pathology in dt

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“…The NH 2 -terminal domain of eBPAG1 is implicated in its recruitment to HDs. This region associates with the cytoplasmic domain of two transmembrane components of HDs, the bullous pemphigoid antigen 2 (BPAG2, also termed BP180) and the integrin ␤4 subunit (9).…”

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confidence: 99%

The Hemidesmosomal Protein Bullous Pemphigoid Antigen 1 and the Integrin β4 Subunit Bind to ERBIN

Favre

Fontao

Koster

et al. 2001

Journal of Biological Chemistry

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The bullous pemphigoid antigen 1 (eBPAG1) is a constituent of hemidesmosomes (HDs), cell-substrate adhesion complexes in stratified epithelia. Although its COOH terminus interacts with intermediate filaments, its NH 2 terminus is important for its recruitment into HDs. To identify proteins that interact with the NH 2 terminus of human eBPAG1, we performed a yeast twohybrid screen, which uncovered a protein belonging to the LAP/LERP (for LRR and PDZ domain) protein family with 16 NH 2 -terminal leucine-rich repeats and a COOH-terminal PDZ domain. The gene for this LAP/ LERP protein comprises at least 26 exons located on the long arm of chromosome 5. In most human tissues, several transcripts were detected differing in the coding region situated upstream of or within the PDZ domain. One of the encoded variants was found to correspond to the recently described protein ERBIN. In yeast and in vitro binding experiments, ERBIN was shown to interact not only with eBPAG1 but also with the COOH-terminal region of the cytoplasmic domain of the integrin ␤4 subunit, another component of HDs. Antibodies raised against the COOH terminus showed that ERBIN is expressed in keratinocytes. In transfected epithelial cells the protein, however, was not localized in HDs but was either diffusely distributed over the cytoplasm or concentrated at the basolateral plasma membrane. Because ERBIN had been shown previously to interact with the transmembrane tyrosine kinase receptor Erb-B2, which in turn associates with the integrin ␤4 subunit, we suggest that ERBIN provides a link between HD assembly and Erb-B2 receptor signaling.Bullous pemphigoid antigen 1 (epithelial BPAG1 or eBPAG1)1 is a component of hemidesmosomes (HDs), multiprotein adhesion complexes promoting cell-substrate adhesion in stratified and complex epithelia. Ultrastructurally, these complexes appear as electron-dense structures in close contact with the basal cell membrane associated with the cytoskeleton (1, 2). eBPAG1 was identified originally as an autoantigen in the autoimmune subepidermal blistering disorder of the skin called bullous pemphigoid (3, 4). This protein is a member of a protein family involved in cytoskeletal organization, the plakins that also comprise desmoplakin, plectin, envoplakin, and periplakin (reviewed in Ref. 5). The structural organization of the plakins is similar, with a central coiled-coil domain responsible for dimerization flanked by two large globular end domains. Although the NH 2 termini of plakins seems to mediate their recruitment to distinct plasma membrane sites (6 -9), their COOH termini are implicated in their attachment to the intermediate filament cytoskeleton (7, 10, 11). Specifically, cell transfection and yeast two-hybrid analyses have demonstrated that the last 768 residues of human eBPAG1 contain sequences important for their interaction with intermediate filaments (7,12). Consistent with this result, BPAG1-knockout mice show discrete signs of blistering, most likely as a result of an impaired attachment of keratin-intermed...

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The N Terminus of the Transmembrane Protein BP180 Interacts with the N-terminal Domain of BP230, Thereby Mediating Keratin Cytoskeleton Anchorage to the Cell Surface at the Site of the Hemidesmosome

Cited by 106 publications

References 39 publications

Spectraplakin family proteins – cytoskeletal crosslinkers with versatile roles

Spectraplakin family proteins – cytoskeletal crosslinkers with versatile roles

Dystonin/Bpag1—A link to what?

The Hemidesmosomal Protein Bullous Pemphigoid Antigen 1 and the Integrin β4 Subunit Bind to ERBIN

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