ArticleBiochimica et biophysica acta2009
Alternatively spliced exon 5 of the FERM domain of protein 4.1R encodes a novel binding site for erythrocyte p55 and is critical for membrane targeting in epithelial cells.
Article in Biochimica et biophysica acta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 29 citations in OpenAlex.
- The function of alternative splicing in the proteome: rewiring protein interactomes to put old functions into new contexts.Nature structural & molecular biology · 2023Review
- Review
- Functional screen of inflammatory bowel disease genes reveals key epithelial functions.Genome medicine · 2021Article
- Article
- Molecular characterization of direct interactions between MPP1 and flotillins.Scientific reports · 2021Article
- Not Just Another Scaffolding Protein Family: The Multifaceted MPPs.Molecules (Basel, Switzerland) · 2020Review
- Epithelial-specific isoforms of protein 4.1R promote adherens junction assembly in maturing epithelia.The Journal of biological chemistry · 2020Article
- The membrane palmitoylated protein, MPP6, is involved in myelin formation in the mouse peripheral nervous system.Histochemistry and cell biology · 2019Article
- Article
- Function of alternative splicing.Gene · 2013Review
- 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
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Direct physical linkage of MAGUKs to the actin cytoskeleton was first established by the interaction of erythrocyte p55 with the FERM domain of protein 4.1R. Subsequently, it was reported that p55 binds to a 51-amino acid peptide, encoded by exon 10, located within the FERM domain of protein 4.1R. In this study, we investigated the nature of the p55-FERM domain binding interface and show that p55 binds to a second 35-amino acid peptide, encoded by an alternatively spliced exon 5, located within the FERM domain of protein 4.1R. Competition and Surface Plasmon Resonance-binding measurements suggest that the peptides encoded by exons 5 and 10 bind to independent sites within the D5 domain of p55. Interestingly, the full length 135 kDa isoform of protein 4.1R containing both exons 5 and 10 was targeted exclusively to the plasma membrane of epithelial cells whereas the same isoform without exon 5 completely lost its membrane localization capacity. Together, these results indicate that p55 binds to two distinct sites within the FERM domain, and the alternatively spliced exon 5 is necessary for the membrane targeting of protein 4.1R in epithelial cells. Since sequences similar to the exon 5-peptide of protein 4.1R and D5 domain of p55 are conserved in many proteins, our findings suggest that a similar mechanism may govern the membrane targeting of other FERM domain containing proteins.
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