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Role of plectin and its interacting molecules in cancer

Medical Oncology, 2023
Plectin, as the cytolinker and scaffolding protein, are widely expressed and abundant in many tissues, and has involved in various cellular activities contributing to tumorigenesis, such as cell adhesion, migration, and signal transduction. Due to the specific expression and differential localization of plectin in cancer, most researchers focus on the ...
jiehui
exaly   +3 more sources

Plectin-related skin diseases

Journal of Dermatological Science, 2015
Plectin has been characterized as a linker protein that is expressed in many cell types and is distinctive in various isoforms in the N-terminus and around the rod domain due to complicated alternative splicing of PLEC, the gene encoding plectin. Plectin deficiency causes autosomal recessive epidermolysis bullosa simplex (EBS) with involvement of the ...
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The interaction of plectin with actin: evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin

Journal of Cell Science, 2001
Plectin is a major component of the cytoskeleton and is expressed in a wide variety of cell types. It plays an important role in the integrity of the cytoskeleton by cross-linking the three filamentous networks and stabilizing cell-matrix and cell-cell contacts.
Fontao, L   +5 more
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Networking and anchoring through plectin: a key to IF functionality and mechanotransduction

Current Opinion in Cell Biology, 2015
Intermediate filaments (IFs) are involved in multiple cellular processes that are essential for the maintenance of cell and tissue integrity as well as response and adaption to stress. Mainly through pathological manifestations in patients and the analysis of genetic mouse models, it became evident that cytolinker proteins of the plakin protein family ...
Gerhard Wiche   +2 more
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Domain Structure and Transcript Diversity of Plectin

The Biological Bulletin, 1998
Plectin, a cytoskeleton-associated protein of exceptionally large size, is abundantly expressed in a wide variety of mammalian tissues and cell types. It is codistributed with different types of intermediate filaments (IFs) and is prominently located at the plasma membrane attachment sites of IFs and of microfilaments, such as hemidesmosomes (Wiche et ...
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Expression of Pork Plectin during Postmortem Aging

Journal of Agricultural and Food Chemistry, 2019
The current study investigated the distribution and degradation of pork plectin during postmortem aging. Longissimus thoracis (LT) muscles from 12 pig carcasses were vacuum-packaged and aged at 4 °C for 0 h, 6 h, 12 h, 1 day, 3 days, 7 days, and 13 days. Immunofluorescence analysis showed that pork plectin was distributed in a honeycomb-like pattern in
Wangang Zhang, Wangang Zhang, Rui Liu
exaly   +3 more sources

Plectin Deficiency Disease

1999
Just over 25 years ago, De Weerdt and Castelain [1] described the combination of progressive muscular weakness and dystrophic epidermolysis bullosa with an autosomal recessive pattern. Niemi et al. [2] described a Finnish sibship with normal parents and 12 members.
Stephanie Lateo   +4 more
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Role of plectin in cytoskeleton organization and dynamics

Journal of Cell Science, 1998
ABSTRACT Plectin and its isoforms are versatile cytoskeletal linker proteins of very large size (>500 kDa) that are abundantly expressed in a wide variety of mammalian tissues and cell types. Earlier studies indicated that plectin molecules were associated with and/or directly bound to subcomponents of all three major cytoskeletal
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Plectin

1999
Abstract Plectin is a versatile cytoskeletal linker protein of high molecular weight (>500 000 Da) that is abundantly expressed in a wide variety of mammalian tissues and cell types. It interacts with all major cytoskeletal filament networks and is a major constituent of plasma membrane-associated junctional complexes (e.g ...
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Brains and brawn: plectin as regulator and reinforcer of the cytoskeleton

BioEssays, 1999
Plectin is a 580 kDa intracellular protein, previously shown to link intermediate filaments with microtubules, actin filaments, and membrane components. Disruption of the plectin gene in humans and in mice results in severe skin blistering and muscular degeneration, consistent with plectin's structural role in stabilizing cells against mechanical force.
P G, Allen, J V, Shah
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