ArticleMolecular biology of the cell2003
Specificity of binding of the plectin actin-binding domain to beta4 integrin.
Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 46 citations in OpenAlex.
- Conditional knockout of ITGB4 in bronchial epithelial cells directs bronchopulmonary dysplasia.Journal of cellular and molecular medicine · 2023Article
- TCN1 Deficiency Inhibits the Malignancy of Colorectal Cancer Cells by Regulating the ITGB4 Pathway.Gut and liver · 2023Article
- Deletion of TMEM268 inhibits growth of gastric cancer cells by downregulating the ITGB4 signaling pathway.Cell death and differentiation · 2019Article
- The Tissue-Engineered Human Psoriatic Skin Substitute: A Valuable In Vitro Model to Identify Genes with Altered Expression in Lesional Psoriasis.International journal of molecular sciences · 2018Article
- The nesprin-cytoskeleton interface probed directly on single nuclei is a mechanically rich system.Nucleus (Austin, Tex.) · 2017Article
- Article
- Plakins, a versatile family of cytolinkers: roles in skin integrity and in human diseases.The Journal of investigative dermatology · 2014Review
- The Bin/amphiphysin/Rvs (BAR) domain protein endophilin B2 interacts with plectin and controls perinuclear cytoskeletal architecture.The Journal of biological chemistry · 2013Article
- Plectin-intermediate filament partnership in skin, skeletal muscle, and peripheral nerve.Histochemistry and cell biology · 2013Review
- Cytoskeleton in motion: the dynamics of keratin intermediate filaments in epithelia.The Journal of cell biology · 2011Review
- The structure of the plakin domain of plectin reveals a non-canonical SH3 domain interacting with its fourth spectrin repeat.The Journal of biological chemistry · 2011Article
- Genetic analyses of integrin signaling.Cold Spring Harbor perspectives in biology · 2011Review
- EGF-induced MAPK signaling inhibits hemidesmosome formation through phosphorylation of the integrin {beta}4.The Journal of biological chemistry · 2010Article
- Plectin isoform-dependent regulation of keratin-integrin alpha6beta4 anchorage via Ca2+/calmodulin.The Journal of biological chemistry · 2009Article
- Structural basis of the interaction between integrin alpha6beta4 and plectin at the hemidesmosomes.The EMBO journal · 2009Article
- Phosphorylation of a novel site on the {beta}4 integrin at the trailing edge of migrating cells promotes hemidesmosome disassembly.Molecular biology of the cell · 2009Article
- Alpha6beta4 integrin and dystroglycan cooperate to stabilize the myelin sheath.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008Article
- Serine phosphorylation of the integrin beta4 subunit is necessary for epidermal growth factor receptor induced hemidesmosome disruption.Molecular biology of the cell · 2007Article
- Integrin beta4 regulates migratory behavior of keratinocytes by determining laminin-332 organization.The Journal of biological chemistry · 2006Article
- Multiple functions of the integrin alpha6beta4 in epidermal homeostasis and tumorigenesis.Molecular and cellular biology · 2006Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plectin is a major component of the cytoskeleton and links the intermediate filament system to hemidesmosomes by binding to the integrin beta4 subunit. Previously, a binding site for beta4 was mapped on the actin-binding domain (ABD) of plectin and binding of beta4 and F-actin to plectin was shown to be mutually exclusive. Here we show that only the ABDs of plectin and dystonin bind to beta4, whereas those of other actin-binding proteins do not. Mutations of the ABD of plectin-1C show that Q131, R138, and N149 are critical for tight binding of the ABD to beta4. These residues form a small cavity, occupied by a well-ordered water molecule in the crystal structure. The beta4 binding pocket partly overlaps with the actin-binding sequence 2 (ABS2), previously shown to be essential for actin binding. Therefore, steric interference may render binding of beta4 and F-actin to plectin mutually exclusive. Finally, we provide evidence indicating that the residues preceding the ABD in plectin-1A and -1C, although unable to mediate binding to beta4 themselves, modulate the binding activity of the ABD for beta4. These studies demonstrate the unique property of the plectin-ABD to bind to both F-actin and beta4, and explain why several other ABD-containing proteins that are expressed in basal keratinocytes are not recruited into hemidesmosomes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.