Plectin: A High-molecular-weight Cytoskeletal Polypeptide Component That Copurifies with Intermediate Filaments of the Vimentin Type

Wiche, Gerhard; Herrmann, Harald; Leichtfried, F E; Pytela, Robert

doi:10.1101/sqb.1982.046.01.044

Cited by 65 publications

(42 citation statements)

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“…The ␣v␤3-integrin associates with a laminin subunit at the core of the structure. We speculate that vimentin-type intermediate filaments interact with the VMA via an association with plectin (Wiche et al, 1982;Steinböck et al, 2000). Because plectin possesses an actin-binding motif, plectin, together with focal contact proteins such as vinculin, may be involved in mediating microfilament (MF) bundle-cell surface association (Elliot et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

“…These may be comparable to the vimentin-associated focal contacts demonstrated by Bershadsky et al (1987) in quail embryo fibroblasts. We assume that plectin mediates the interaction of vimentin with these focal contact-like devices, based on its known vimentin-binding properties, its localization, and its function in linking other types of intermediate filaments to the cell surface (Wiche et al, 1982;Steinbö ck and Wiche, 1999). Plectin, via its actin-binding domain, may also facilitate microfilament-cell surface binding at the basal surface of endothelial cells (Elliot et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

“…polyclonal antiserum against ␣v-integrin, a major cell surface matrix receptor expressed by endothelial cells in vitro and in vivo (Figure 2, A-C) (Brooks et al, 1994(Brooks et al, -1995Varner, 1997). In TrHBMECs, ␣v integrin antibody colocalizes with staining generated by probes against the ␣v␤3 integrin complex, the focal contact protein vinculin and plectin, and a cytoskeleton cross-linking protein (Wiche et al, 1982;Wiche 1998) (Figure 2, D-F, G-I, and J-L, respectively). Thus, the vinculin-positive, plectin-positive focal contacts in TrHBMECs are enriched in ␣v␤3 integrin heterodimers.…”

Section: Immunofluorescence Analyses Of Endothelial Cellsmentioning

confidence: 99%

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Structure and Function of a Vimentin-associated Matrix Adhesion in Endothelial Cells

Gonzales

Weksler

Tsuruta

et al. 2001

MBoC

148

134

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The ␣4 laminin subunit is a component of endothelial cell basement membranes. An antibody (2A3) against the ␣4 laminin G domain stains focal contact-like structures in transformed and primary microvascular endothelial cells (TrHBMECs and HMVECs, respectively), provided the latter cells are activated with growth factors. The 2A3 antibody staining colocalizes with that generated by ␣v and ␤3 integrin antibodies and, consistent with this localization, TrHBMECs and HMVECs adhere to the ␣4 laminin subunit G domain in an ␣v␤3-integrin-dependent manner. The ␣v␤3 integrin/2A3 antibody positively stained focal contacts are recognized by vinculin antibodies as well as by antibodies against plectin. Unusually, vimentin intermediate filaments, in addition to microfilament bundles, interact with many of the ␣v␤3 integrin-positive focal contacts. We have investigated the function of ␣4-laminin and ␣v␤3-integrin, which are at the core of these focal contacts, in cultured endothelial cells. Antibodies against these proteins inhibit branching morphogenesis of TrHBMECs and HMVECs in vitro, as well as their ability to repopulate in vitro wounds. Thus, we have characterized an endothelial cell matrix adhesion, which shows complex cytoskeletal interactions and whose assembly is regulated by growth factors. Our data indicate that this adhesion structure may play a role in angiogenesis.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Immunofluorescence Analyses Of Endothelial Cellsmentioning

confidence: 99%

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Structure and Function of a Vimentin-associated Matrix Adhesion in Endothelial Cells

Gonzales

Weksler

Tsuruta

et al. 2001

MBoC

148

134

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“…Plectin, a member of the plakin family of cytolinker proteins, was originally identified as an abundant IFassociated protein in C6 glioma cells 5 and has subsequently been characterized as a ubiquitously expressed cytoskeletal cross-linker. 6 It is localized at the cytoskeleton-plasma membrane interface and binds IFs, actin microfilaments, microtubules, and integrins.…”

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confidence: 99%

Plectin Regulates the Organization of Glial Fibrillary Acidic Protein in Alexander Disease

Tian

Gregor

Wiche

et al. 2006

The American Journal of Pathology

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Alexander disease (AxD) is a rare but fatal neurological disorder caused by mutations in the astrocytespecific intermediate filament protein glial fibrillary acidic protein (GFAP). Histologically, AxD is characterized by cytoplasmic inclusion bodies called Rosenthal fibers (RFs), which contain GFAP, small heat shock proteins, and other undefined components. Here, we describe the expression of the cytoskeletal linker protein plectin in the AxD brain. RFs displayed positive immunostaining for plectin and GFAP, both of which were increased in the AxD brain. Co-localization, co-immunoprecipitation, and in vitro overlay analyses demonstrated direct interaction of plectin and GFAP. GFAP with the most common AxD mutation, R239C (RC GFAP), mainly formed abnormal aggregates in human primary astrocytes and murine plectin-deficient fibroblasts. Transient transfection of full-length plectin cDNA converted these aggregates to thin filaments, which exhibited diffuse cytoplasmic distribution. Compared to wild-type GFAP expression, RC GFAP expression lowered plectin levels in astrocytoma-derived stable transfectants and plectin-positive fibroblasts. A much higher proportion of total GFAP was found in the Triton X-insoluble fraction of plectin-deficient fibroblasts than in wild-type fibroblasts. Taken together, our results suggest that insufficient amounts of plectin, due to RC GFAP expression, promote GFAP aggregation and RF formation in AxD.

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“…More restricted in their expression, periplakin and envoplakin cross link desmosomes and IFs to the cornified envelope of terminally differentiating cells of stratified squamous epithelia (Ruhrberg et al 1996). One of the most versatile and ubiquitously expressed plakins is plectin, which decorates cytoplasmic IF networks and also binds to hemidesmosomes and desmosomes, MAPs, ␣-spectrin, actin filaments, and the nuclear envelope (Wiche et al 1982;Andra et al 1997Andra et al , 1998Rezniczek et al 1998;Schaapveld et al 1998). The association of plakins with IFs changes on the phosphorylation state of serine residues in the carboxy-terminal segment of the plakin, suggesting that this interaction may be regulated within cells.…”

Section: Introducing the Plakins As Intermediate Filament Linker Protmentioning

confidence: 99%

Bridging cytoskeletal intersections

Fuchs¹,

2001

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Plectin: A High-molecular-weight Cytoskeletal Polypeptide Component That Copurifies with Intermediate Filaments of the Vimentin Type

Cited by 65 publications

References 0 publications

Structure and Function of a Vimentin-associated Matrix Adhesion in Endothelial Cells

Structure and Function of a Vimentin-associated Matrix Adhesion in Endothelial Cells

Plectin Regulates the Organization of Glial Fibrillary Acidic Protein in Alexander Disease

Bridging cytoskeletal intersections

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