Comparative structural analysis of desmoplakin, bullous pemphigoid antigen and plectin: members of a new gene family involved in organization of intermediate filaments

Green, Kathleen J.; Virata, M. L.A.; Elgart, George W.; Stanley, John R.

doi:10.1016/s0141-8130(05)80004-2

Cited by 168 publications

(127 citation statements)

References 27 publications

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“…Only a few studies have also addressed the fate of IF-associated proteins during mitosis. IFAP 300, a protein that is immunologically related to plectin (Herrmann and Wiche, 1987;Skalli et al, 1994) and possibly represents a member of the plectin, desmoplakin, and bullous pemphigoid antigen gene family Green et al, 1992), similar to plectin, has been shown to become phosphorylated in mitosis at a unique site, which also serves as target site for purified p34cdc2 kinase. However, because IFAP 300 has been shown to remain closely associated with IFs during mitosis (Skalli et al, 1992a), the function of mitosis-specific phosphorylation of IFAP 300 is not yet clear.…”

Section: Discussionmentioning

confidence: 99%

M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase.

Foisner

Malecz

Dressel

et al. 1996

MBoC

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Plectin, a widespread and abundant cytoskeletal cross-linking protein, serves as a target for protein kinases throughout the cell cycle, without any significant variation in overall phosphorylation level. One of the various phosphorylation sites of the molecule was found to be phosphorylated preferentially during mitosis. By in vivo phosphorylation of ectopically expressed plectin domains in stably transfected Chinese hamster ovary cells, this site was mapped to the C-terminal repeat 6 domain of the polypeptide. The same site has been identified as an in vitro target for p34cdc2 kinase. Mitosis-specific phosphorylation of plectin was accompanied by a rearrangement of plectin structures, changing from a filamentous, largely vimentin-associated state in interphase to a diffuse vimentin-independent distribution in mitosis as visualized by immunofluorescence microscopy. Subcellular fractionation studies showed that in interphase cells up to 80% of cellular plectin was found associated with an insoluble cell fraction mostly consisting of intermediate filaments, while during mitosis the majority of plectin (> 75%) became soluble. Furthermore, phosphorylation of purified plectin by p34cdc2 kinase decreased plectin's ability to interact with preassembled vimentin filaments in vitro. Together, our data suggest that a mitosis-specific phosphorylation involving p34cdc2 kinase regulates plectin's cross-linking activities and association with intermediate filaments during the cell cycle.

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Section: Discussionmentioning

confidence: 99%

M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase.

Foisner

Malecz

Dressel

et al. 1996

MBoC

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“…Desmoplakin is among the founding members of a large family of proteins termed the plakin family of cytolinkers (Green et al 1992b;Sonnenberg and Liem 2007). These large molecules link cytoskeletal networks to the plasma membrane and integrate actin, microtubules, and intermediate filaments.…”

Section: Desmoplakinmentioning

confidence: 99%

The Desmosome

Delva¹,

Tucker²,

Kowalczyk³

2009

Cold Spring Harbor Perspectives in Biology

348

310

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“…BP230 autoantibodies bind to a specific site within the cytoplasmic plaque of the hemidesmosome to which keratin bundles attach (Klatte et al, 1989). Molecular characterization of BP230 has demonstrated that it belongs to the "plakin" family of proteins and is related to the intermediate filament-binding proteins desmoplakin and plectin (Sawamura et al, 1991;Tanaka et al, 1991;Green et al, 1992;Ruhrberg and Watt, 1997). Like desmoplakin and plectin, BP230 can interact directly with keratin filaments, as shown by Fuchs and coworkers (Guo et al, 1995).…”

Section: Introductionmentioning

confidence: 97%

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

Jones

2000

MBoC

106

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In epidermal cells, the keratin cytoskeleton interacts with the elements in the basement membrane via a multimolecular junction called the hemidesmosome. A major component of the hemidesmosome plaque is the 230-kDa bullous pemphigoid autoantigen (BP230/BPAG1), which connects directly to the keratin-containing intermediate filaments of the cytoskeleton via its C terminus. A second bullous pemphigoid antigen of 180 kDa (BP180/BPAG2) is a type II transmembrane component of the hemidesmosome. Using yeast two-hybrid technology and recombinant proteins, we show that an N-terminal fragment of BP230 can bind directly to an N-terminal fragment of BP180. We have also explored the consequences of expression of the BP230 N terminus in 804G cells that assemble hemidesmosomes in vitro. Unexpectedly, this fragment disrupts the distribution of BP180 in transfected cells but has no apparent impact on the organization of endogenous BP230 and ␣6␤4 integrin. We propose that the BP230 N terminus competes with endogenous BP230 protein for BP180 binding and inhibits incorporation of BP180 into the cell surface at the site of the hemidesmosome. These data provide new insight into those interactions of the molecules of the hemidesmosome that are necessary for its function in integrating epithelial and connective tissue types.

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Comparative structural analysis of desmoplakin, bullous pemphigoid antigen and plectin: members of a new gene family involved in organization of intermediate filaments

Cited by 168 publications

References 27 publications

M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase.

M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase.

The Desmosome

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

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