Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Molecular mechanism of intermediate filament recognition by plakin proteins.

Biochimica et biophysica acta. Molecular cell research - 1 Nov 2020

Mohammed Fiyaz, Trieber Catharine, Overduin Michael, Chidgey Martyn

Abstract excerpt

The plakin family of cytolinkers interacts with intermediate filaments (IFs) through plakin repeat domain (PRD) and linker modules. Recent structure/function studies have established the molecular basis of envoplakin-PRD and periplakin-linker interactions with vimentin. Both plakin modules share a broad basic groove which recognizes acidic rod elements on IFs, a mechanism that is applicable to other plakin family...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Arrhythmogenic Right Ventricular Dysplasia

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Intermediate Filaments

Share to Mutation

Share to Protein Binding

Share to Protein Domains

Share to Skin and Cellular Biology Research

Share to Vimentin

Source

Identifiers

PMID: 32712070
DOI: 10.1016/j.bbamcr.2020.118801

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular mechanism of intermediate filament recognition by plakin proteins.PMID 32712070Read ↗

Missense Mutations in Desmoplakin Plakin Repeat Domains Have Dramatic Effects on Domain Structure and Function.Semantic proximity Read ↗

Plectin-intermediate filament partnership in skin, skeletal muscle, and peripheral nerve.Semantic proximity Read ↗

The plakin family: versatile organizers of cytoskeletal architectureSemantic proximity Read ↗

Unique role for the periplakin tail in intermediate filament association: specific binding to keratin 8 and vimentinSemantic proximity Read ↗

The nonlinear structure of the desmoplakin plakin domain and the effects of cardiomyopathy-linked mutations.Semantic proximity Read ↗

Desmoplakin CSM models unravel mechanisms regulating the binding to intermediate filaments and putative therapeutics for cardiocutaneous diseasesSemantic proximity Read ↗

Interaction of periplakin and envoplakin with intermediate filamentsSemantic proximity Read ↗

The many faces of plectin and plectinopathies: pathology and mechanisms.Semantic proximity Read ↗

Interaction of plectin with keratins 5 and 14: dependence on several plectin domains and keratin quaternary structure.Semantic proximity Read ↗

Desmoplakin CSM models unravel mechanisms regulating the binding to intermediate filaments and putative therapeutics for cardiocutaneous diseases.Semantic proximity Read ↗

Cytolinker cross-talk: Periplakin N-terminus interacts with plectin to regulate keratin organisation and epithelial migrationSemantic proximity Read ↗

Arrhythmogenic Right Ventricular Cardiomyopathy Plakophilin-2 Mutations Disrupt Desmosome Assembly and StabilitySemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.