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Structure and hydrodynamic properties of plectin molecules

Journal of Molecular Biology, 1987
Plectin is a cytoskeletal, high molecular weight protein of widespread and abundant occurrence in cultured cells and tissues. To study its molecular structure, the protein was purified from rat glioma C6 cells and subjected to chemical and biophysical analyses.
R, Foisner, G, Wiche
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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 Di, Li Hailong
exaly   +3 more sources

Determining the mechanical properties of plectin in mouse myoblasts and keratinocytes

open access: yesExperimental Cell Research, 2015
Plectin is the prototype of an intermediate filament (IF)-based cytolinker protein. It affects cells mechanically by interlinking and anchoring cytoskeletal filaments and acts as scaffolding and docking platform for signaling proteins to control ...
Navid Bonakdar   +2 more
exaly   +2 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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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, Qin Hou, 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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