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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/23063
Title: Analysis of the interaction between human kidney anion exchanger 1 and kanadaptin using yeast two-hybrid systems
Authors: Phonphimon Wongthida
Varaporn Akkarapatumwong
Thawornchai Limjindaporn
Saranya Kittanakom
Thitima Keskanokwong
Lily Eurwilaichitr
Pa Thai Yenchitsomanus
Mahidol University
Thailand National Center for Genetic Engineering and Biotechnology
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 24-Mar-2006
Citation: Genetics and Molecular Biology. Vol.29, No.1 (2006), 14-22
Abstract: Kidney anion exchanger adaptor protein (Kanadaptin) is a protein which interacts with the cytoplasmic N-terminal domain of kidney anion exchanger 1 (kAE1) and was first detected in mice using the yeast two-hybrid system and was also found to co-localize with kAE1 in rabbit α-intercalated cells. Impaired trafficking of human kAE1 can result in the kidney disease-distal renal tubular acidosis (dRTA), and defective interaction between human kAE1 and kanadaptin may cause this trafficking impairment and be the basis for dRTA pathogenesis. However, it is unknown whether kAE1 can really interact with kanadaptin in humans. We have thus investigated the interaction between human kAE1 and human kanadaptin by using both Gal4 and LexA yeast two-hybrid systems. It was found that co-expression of Gal4DBD fused to the cytoplasmic N-terminal domain of kAE1 and Gal4AD fused to kanadaptin could not activate the transcription of the ADE2, HIS3 and lacZ reporters in the Gal4 system. A similar result was obtained for the interaction between B42AD fused to the cytoplasmic N-terminal domain of kAE1 and LexA fused to kanadaptin in activation of lacZ transcription in the LexA system. The absence of interaction between the fusion proteins in both yeast two-hybrid systems raises the possibility that kAE1 may not interact with kanadaptin in human cells. Considerably different structures of both kAE1 and kanadaptin in mice and humans may lead to different binding properties of the proteins in these two species. Copyright by the Brazilian Society of Genetics.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=33645026171&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/23063
ISSN: 16784685
14154757
Appears in Collections:Scopus 2006-2010

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