ArticleProceedings of the National Academy of Sciences of the United States of America1987
Regulated expression of multiple chicken erythroid membrane skeletal protein 4.1 variants is governed by differential RNA processing and translational control.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 48 citations in OpenAlex.
- Deciphering the nuclear import pathway for the cytoskeletal red cell protein 4.1R.Molecular biology of the cell · 1999Article
- Role of tissue specific alternative pre-mRNA splicing in the differentiation of the erythrocyte membrane.Transactions of the American Clinical and Climatological Association · 1997Review
- Protein 4.1 is a component of the nuclear matrix of mammalian cells.The Biochemical journal · 1995Article
- v-jun cooperates with v-erbB to transform the thrombocytic/megakaryocytic lineage.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Characterization of isoforms of protein 4.1 present in the nucleus.The Biochemical journal · 1991Article
- Heterogeneity of mRNA and protein products arising from the protein 4.1 gene in erythroid and nonerythroid tissues.The Journal of cell biology · 1990Article
- Molecular cloning of human protein 4.2: a major component of the erythrocyte membrane.Proceedings of the National Academy of Sciences of the United States of America · 1990Article
- Selective expression of an erythroid-specific isoform of protein 4.1.Proceedings of the National Academy of Sciences of the United States of America · 1988Article
- Alternative primary structures in the transmembrane domain of the chicken erythroid anion transporter.Molecular and cellular biology · 1988Article
- Erythroid anion transporter assembly is mediated by a developmentally regulated recruitment onto a preassembled membrane cytoskeleton.The Journal of cell biology · 1987Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Protein 4.1 is an extrinsic membrane protein that facilitates the interaction of spectrin and actin in the erythroid membrane skeleton and exists as several structurally related polypeptides in chickens. The ratio of protein 4.1 variants is developmentally regulated during terminal differentiation of chicken erythroid and lenticular cells. To examine the mechanisms by which multiple chicken protein 4.1 variants are differentially expressed, we have isolated cDNA clones specific for chicken erythroid protein 4.1. We show that a single protein 4.1 gene gives rise to multiple 6.6-kilobase mRNAs by differential RNA processing. Furthermore, the ratios of protein 4.1 mRNAs change during chicken embryonic erythropoiesis. We observe a quantitative difference in variant ratios when protein 4.1 is synthesized in vivo or in a rabbit reticulocyte lysate in vitro. Our results show that the expression of multiple protein 4.1 polypeptides is regulated at the levels of translation and RNA processing.
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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.