ArticleThe Journal of biological chemistry2011
The structure of the plakin domain of plectin reveals a non-canonical SH3 domain interacting with its fourth spectrin repeat.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 49 citations in OpenAlex.
- Mechanics of cell sheets: plectin as an integrator of cytoskeletal networks.Open biology · 2025Review
- Gustavson syndrome is caused by an in-frame deletion in RBMX associated with potentially disturbed SH3 domain interactions.European journal of human genetics : EJHG · 2024Article
- Effects of Copy Number Variations in the Plectin (Animals : an open access journal from MDPI · 2023Article
- Role of plectin and its interacting molecules in cancer.Medical oncology (Northwood, London, England) · 2023Review
- A Systematic Compilation of Human SH3 Domains: A Versatile Superfamily in Cellular Signaling.Cells · 2023Review
- Ancient Origins of Cytoskeletal Crosstalk: Spectraplakin-like Proteins Precede the Emergence of Cortical Microtubule Stabilization Complexes as Crosslinkers.International journal of molecular sciences · 2022Article
- Review
- Review
- The plakin domain ofDevelopment (Cambridge, England) · 2019Article
- Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics.The Journal of biological chemistry · 2018Article
- The mechano-sensing role of the unique SH3 insertion in plakin domains revealed by Molecular Dynamics simulations.Scientific reports · 2017Article
- Epidermolysis bullosa simplex in sibling Eurasier dogs is caused by a PLEC non-sense variant.Veterinary dermatology · 2017Article
- Defenders and Challengers of Endothelial Barrier Function.Frontiers in immunology · 2017Review
- The Structure of the Plakin Domain of Plectin Reveals an Extended Rod-like Shape.The Journal of biological chemistry · 2016Article
- In vivo epidermal migration requires focal adhesion targeting of ACF7.Nature communications · 2016Article
- Plakins, a versatile family of cytolinkers: roles in skin integrity and in human diseases.The Journal of investigative dermatology · 2014Review
- Article
- Intermediate filament-associated cytolinker plectin 1c destabilizes microtubules in keratinocytes.Molecular biology of the cell · 2013Article
- Structural organization of the nine spectrin repeats of Kalirin.Biochemistry · 2012Article
- Spectraplakins: master orchestrators of cytoskeletal dynamics.The Journal of cell biology · 2012Review
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Authors and funding
4 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plectin belongs to the plakin family of cytoskeletal crosslinkers, which is part of the spectrin superfamily. Plakins contain an N-terminal conserved region, the plakin domain, which is formed by an array of spectrin repeats (SR) and a Src-homology 3 (SH3), and harbors binding sites for junctional proteins. We have combined x-ray crystallography and small angle x-ray scattering (SAXS) to elucidate the structure of the central region of the plakin domain of plectin, which corresponds to the SR3, SR4, SR5, and SH3 domains. The crystal structures of the SR3-SR4 and SR4-SR5-SH3 fragments were determined to 2.2 and 2.95 Å resolution, respectively. The SH3 of plectin presents major alterations as compared with canonical Pro-rich binding SH3 domains, suggesting that plectin does not recognize Pro-rich motifs. In addition, the SH3 binding site is partially occluded by an intramolecular contact with the SR4. Residues of this pseudo-binding site and the SR4/SH3 interface are conserved within the plakin family, suggesting that the structure of this part of the plectin molecule is similar to that of other plakins. We have created a model for the SR3-SR4-SR5-SH3 region, which agrees well with SAXS data in solution. The three SRs form a semi-flexible rod that is not altered by the presence of the SH3 domain, and it is similar to those found in spectrins. The flexibility of the plakin domain, in analogy with spectrins, might contribute to the role of plakins in maintaining the stability of tissues subject to mechanical stress.
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