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Direct interaction and cooperative role of tumor suppressor p16 with band 3 (AE1)
By using the C-terminal 112-residue of band 3 to screen the K562 cDNA library, we find that the p16 interacts with band 3, which was confirmed both in yeast and in mammalian cells. Functional experiments show that p16 facilitates the movement of band 3 to plasma membrane with increased anion transpo...
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Published in: | FEBS letters 2005-04, Vol.579 (10), p.2105-2110 |
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container_title | FEBS letters |
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creator | Fu, Guo-Hui Wang, Yong Xi, Yu-Hui Shen, Wei-Wei Pan, Xiao-Yan Shen, Wu-Zhong Jiang, Xiao-Shu Chen, Guo-Qiang |
description | By using the C-terminal 112-residue of band 3 to screen the K562 cDNA library, we find that the p16 interacts with band 3, which was confirmed both in yeast and in mammalian cells. Functional experiments show that p16 facilitates the movement of band 3 to plasma membrane with increased anion transport activity in 293t cells. Moreover, expression of endogenous p16 in 293t cells was increased at 24 and 36
h after transfection with band 3. Our findings provide a novel regulation pathway for both band 3 and p16. |
doi_str_mv | 10.1016/j.febslet.2005.02.063 |
format | article |
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h after transfection with band 3. 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subjects | 6-methoxy-N-(3-sulfopropyl)quinolinium Amino Acid Sequence Anion Exchange Protein 1, Erythrocyte - metabolism Anion exchanger Anion transport activity Band 3 Blotting, Western CA II carbonic anhydrase II CAT Cell Line chloramphenicol acetyltransferase Cyclin-Dependent Kinase Inhibitor p16 - metabolism Humans Immunohistochemistry Immunoprecipitation Molecular Sequence Data p16 PLP Protein Binding pyridoxal phosphate SPQ Two-Hybrid System Techniques |
title | Direct interaction and cooperative role of tumor suppressor p16 with band 3 (AE1) |
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