Your browser doesn't support javascript.
loading
Analysis of the interaction between human kidney anion exchanger 1 and kanadaptin using yeast two-hybrid systems
Wongthida, Phonphimon; Akkarapatumwong, Varaporn; Limjindaporn, Thawornchai; Kittanakom, Saranya; Keskanokwong, Thitima; Eurwilaichitr, Lily; Yenchitsomanus, Pa-Thai.
  • Wongthida, Phonphimon; Mahidol University. Institute of Molecular Biology and Genetics. Nakhon Pathom. TH
  • Akkarapatumwong, Varaporn; Mahidol University. Institute of Molecular Biology and Genetics. Nakhon Pathom. TH
  • Limjindaporn, Thawornchai; Mahidol University. Siriraj Hospital. Faculty of Medicine. Department of Anatomy. Bangkok. TH
  • Kittanakom, Saranya; Mahidol University. Siriraj Hospital. Faculty of Medicine. Department of Research and Development. Bangkok. TH
  • Keskanokwong, Thitima; Mahidol University. Institute of Molecular Biology and Genetics. Nakhon Pathom. TH
  • Eurwilaichitr, Lily; BIOTEC Central Research Unit. Klongluang. TH
  • Yenchitsomanus, Pa-Thai; Mahidol University. Siriraj Hospital. Faculty of Medicine. Department of Research and Development. Bangkok. TH
Genet. mol. biol ; 29(1): 14-22, 2006. ilus, tab, graf
Artículo en Inglés | LILACS | ID: lil-423413
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 a-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.
Asunto(s)
Texto completo: Disponible Índice: LILACS (Américas) Asunto principal: Saccharomyces cerevisiae / Acidosis Tubular Renal / Proteína 1 de Intercambio de Anión de Eritrocito Límite: Animales / Humanos Idioma: Inglés Revista: Genet. mol. biol Asunto de la revista: Genética Año: 2006 Tipo del documento: Artículo País de afiliación: Tailandia Institución/País de afiliación: BIOTEC Central Research Unit/TH / Mahidol University/TH

Similares

MEDLINE

...
LILACS

LIS

Texto completo: Disponible Índice: LILACS (Américas) Asunto principal: Saccharomyces cerevisiae / Acidosis Tubular Renal / Proteína 1 de Intercambio de Anión de Eritrocito Límite: Animales / Humanos Idioma: Inglés Revista: Genet. mol. biol Asunto de la revista: Genética Año: 2006 Tipo del documento: Artículo País de afiliación: Tailandia Institución/País de afiliación: BIOTEC Central Research Unit/TH / Mahidol University/TH