Four variant chicken erythroid AE1 anion exchangers. Role of the alternative N-terminal sequences in intracellular targeting in transfected human erythroleukemia cells
| Autor: | K H, Cox, T L, Adair-Kirk, J V, Cox |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Intracellular Fluid
Erythrocytes Base Sequence Molecular Sequence Data Genetic Variation DNA Transfection Immunohistochemistry Polymerase Chain Reaction Anion Exchange Protein 1 Erythrocyte Tumor Cells Cultured Animals Humans Amino Acid Sequence Leukemia Erythroblastic Acute RNA Messenger Promoter Regions Genetic Chickens Signal Transduction Subcellular Fractions |
| Zdroj: | The Journal of biological chemistry. 270(34) |
| ISSN: | 0021-9258 |
| Popis: | Four variant AE1 anion exchangers with predicted molecular masses of approximately 99, approximately 102, approximately 104, and approximately 108 kDa are expressed in chicken erythroid cells. These variant polypeptides differ in sequence only at the N terminus of their cytoplasmic domains. Molecular analyses have shown that transcripts derived from both of the erythroid-specific promoters, P1 and P2, encode all four of these AE1 anion exchanger variants. However, quantitative RNase protection analyses have shown that the transcripts derived from the P1 promoter are much more prevalent than those derived from the P2 promoter. Reverse transcriptase polymerase chain reaction studies have indicated that the extensive diversity in the transcripts derived from the AE1 gene occurs both in primitive and definitive lineage erythroid cells. Transient transfection analyses using human erythroleukemia cells have investigated the functional significance of the alternative sequences at the N terminus of these variant exchangers. These studies have shown that the erythroid AE1 variants are sorted to different membrane compartments in these cells. The approximately 99- and approximately 102-kDa variants are primarily sorted to the plasma membrane, whereas the approximately 108-kDa variant is retained in a perinuclear compartment. These results suggest that the alternative N-terminal cytoplasmic sequences of these polypeptides may serve as signals to direct these variant transporters to different membrane compartments within cells. |
| Databáze: | OpenAIRE |
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