ArticleThe Journal of cell biology1995
Mechanochemistry of protein 4.1's spectrin-actin-binding domain: ternary complex interactions, membrane binding, network integration, structural strengthening.
Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
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Who cites it
42 citing papers in PubMed, 108 citations in OpenAlex.
- The membrane-actin linker ezrin acts as a sliding anchor.Science advances · 2022Article
- Scaffold protein Lin7 family in membrane skeletal protein complex in mouse seminiferous tubules.Histochemistry and cell biology · 2019Article
- RNA splicing during terminal erythropoiesis.Current opinion in hematology · 2017Review
- Mechanoaccumulative Elements of the Mammalian Actin Cytoskeleton.Current biology : CB · 2016Article
- Feisty filaments: actin dynamics in the red blood cell membrane skeleton.Current opinion in hematology · 2016Review
- Direct Cytoskeleton Forces Cause Membrane Softening in Red Blood Cells.Biophysical journal · 2015Article
- CEACAM1 long cytoplasmic domain isoform is associated with invasion and recurrence of hepatocellular carcinoma.Annals of surgical oncology · 2014Article
- Comprehensive characterization of protein 4.1 expression in epithelium of large intestine.Histochemistry and cell biology · 2014Article
- A dynamic alternative splicing program regulates gene expression during terminal erythropoiesis.Nucleic acids research · 2014Article
- Article
- Essential function of protein 4.1G in targeting of membrane protein palmitoylated 6 into Schmidt-Lanterman incisures in myelinated nerves.Molecular and cellular biology · 2012Article
- Intertwined αβ spectrin meeting helical actin protofilament in the erythrocyte membrane skeleton: wrap-around vs. point-attachment.Annals of biomedical engineering · 2011Article
- Phosphorylation-dependent perturbations of the 4.1R-associated multiprotein complex of the erythrocyte membrane.Biochemistry · 2011Article
- Cysteine shotgun-mass spectrometry (CS-MS) reveals dynamic sequence of protein structure changes within mutant and stressed cells.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Erythrocyte tropomodulin isoforms with and without the N-terminal actin-binding domain.The Journal of biological chemistry · 2010Article
- Comprehensive characterization of expression patterns of protein 4.1 family members in mouse adrenal gland: implications for functions.Histochemistry and cell biology · 2010Article
- The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life.Protoplasma · 2010Review
- Article
- Molecular epitopes of the ankyrin-spectrin interaction.Biochemistry · 2008Article
- Dematin and adducin provide a novel link between the spectrin cytoskeleton and human erythrocyte membrane by directly interacting with glucose transporter-1.The Journal of biological chemistry · 2008Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Mechanical strength of the red cell membrane is dependent on ternary interactions among the skeletal proteins, spectrin, actin, and protein 4.1. Protein 4.1's spectrin-actin-binding (SAB) domain is specified by an alternatively spliced exon encoding 21 amino acid (aa) and a constitutive exon encoding 59 aa. A series of truncated SAB peptides were engineered to define the sequences involved in spectrin-actin interactions, and also membrane strength. Analysis of in vitro supramolecular assemblies showed that gelation activity of SAB peptides correlates with their ability to recruit a critical amount of spectrin into the complex to cross-link actin filaments. Also, several SAB peptides appeared to exhibit a weak, cooperative actin-binding activity which mapped to the first 26 residues of the constitutive 59 aa. Fluorescence-imaged microdeformation was used to show SAB peptide integration into the elastic skeletal network of spectrin, actin, and protein 4.1. In situ membrane-binding and membrane-strengthening abilities of the SAB peptides correlated with their in vitro gelation activity. The findings imply that sites for strong spectrin binding include both the alternative 21-aa cassette and a conserved region near the middle of the 59 aa. However, it is shown that only weak SAB affinity is necessary for physiologically relevant action. Alternatively spliced exons can thus translate into strong modulation of specific protein interactions, economizing protein function in the cell without, in and of themselves, imparting unique function.
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Registered trials
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.