ArticleProceedings of the National Academy of Sciences of the United States of America1991
Phosphorylation of protein 4.1 on tyrosine-418 modulates its function in vitro.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 71 citations in OpenAlex.
- Phosphoproteomics and morphology of stored human red blood cells treated by protein tyrosine phosphatases inhibitor.Blood advances · 2024Article
- Development of Mechanical Stability in Late-Stage Embryonic Erythroid Cells: Insights From Fluorescence Imaged Micro-Deformation Studies.Frontiers in physiology · 2021Article
- OsteoBLAST: Computational Routine of Global Molecular Analysis Applied to Biomaterials Development.Frontiers in bioengineering and biotechnology · 2020Article
- Cetuximab and biomarkers in non-small-cell lung carcinoma.Biologics : targets & therapy · 2012Article
- Phosphorylation-dependent perturbations of the 4.1R-associated multiprotein complex of the erythrocyte membrane.Biochemistry · 2011Article
- Cytoskeletal protein 4.1R negatively regulates T-cell activation by inhibiting the phosphorylation of LAT.Blood · 2009Article
- Inhibition of protein 4.1 R and NuMA interaction by mutagenization of their binding-sites abrogates nuclear localization of 4.1 R.Clinical and translational science · 2009Article
- Regulated Fox-2 isoform expression mediates protein 4.1R splicing during erythroid differentiation.Blood · 2008Article
- Mitotic regulation of protein 4.1R involves phosphorylation by cdc2 kinase.Molecular biology of the cell · 2005Article
- A nonerythroid isoform of protein 4.1R interacts with components of the contractile apparatus in skeletal myofibers.Molecular biology of the cell · 2000Article
- A nonerythroid isoform of protein 4.1R interacts with the nuclear mitotic apparatus (NuMA) protein.The Journal of cell biology · 1999Article
- Characterization of the hypertonically induced tyrosine phosphorylation of erythrocyte band 3.The Biochemical journal · 1998Article
- Structural protein 4.1 in the nucleus of human cells: dynamic rearrangements during cell division.The Journal of cell biology · 1997Article
- Mechanochemistry of protein 4.1's spectrin-actin-binding domain: ternary complex interactions, membrane binding, network integration, structural strengthening.The Journal of cell biology · 1995Article
- Homozygous 4.1(-) hereditary elliptocytosis associated with a point mutation in the downstream initiation codon of protein 4.1 gene.The Journal of clinical investigation · 1992Article
- Tyrosine phosphorylation of a membrane protein from Pseudomonas solanacearum.Journal of bacteriology · 1992Article
- Alteration of the kinetic properties of the epidermal growth factor receptor tyrosine kinase by basic proteins.The Biochemical journal · 1992Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Protein 4.1 was initially characterized as a protein that regulates cytoskeletal assembly in erythrocytes. However, recent studies have shown that protein 4.1 is ubiquitous in mammalian cells. Here, we show that protein 4.1 is phosphorylated on tyrosine by the epidermal growth factor receptor (EGFR) tyrosine kinase. The phosphorylation site has been localized to the 8-kDa domain, which has one tyrosine, tyrosine-418. The 8-kDa region is required for the assembly of the spectrin/actin complex, and phosphorylation by EGFR reduced the ability of protein 4.1 to promote the assembly of the spectrin/actin/protein 4.1 ternary complex. Immunoblotting with anti-phosphotyrosine antibodies showed that purified protein 4.1 contained phosphorylated tyrosine, and this increased upon phosphorylation by EGFR. This suggests that tyrosine phosphorylation of protein 4.1 occurs in vivo and may be functionally significant. The tyrosine phosphorylation site is in the center of a sequence motif that is expressed by a differentiation-specific splicing mechanism.
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