Cytoskeletal protein 4.1G binds to the third intracellular loop of the A1 adenosine receptor and inhibits receptor action

Dongcheng Lu, Henglin Yan, Timothy Othman, Christopher P. Turner, Thomas Woolf, Scott A. Rivkees

Research output: Contribution to journalArticle

Abstract

To identify binding partners of the A1AR (A1 adenosine receptor), yeast two-hybrid screening of a rat embryonic cDNA library was performed. This procedure led to the identification of erythrocyte membrane cytoskeletal protein (represented as 4.1G) as an A1AR-binding partner. Truncation studies revealed that the C-terminal domain of 4.1G was essential for binding to A1ARs and that the C-terminal domain of 4. 1G and the third intracellular loop of A1ARs interacted. A 1AR-4.1G interaction was also confirmed in studies using brain tissue. Studies in HEK-293 (human embryonic kidney 293) cells and Chinese-hamster ovary cells showed that 4.1G interfered with A1AR signal transduction, as 4.1G reduced A1AR-mediated inhibition of cAMP accumulation and intracellular calcium release. 4.1G also altered cell-surface A1AR expression. These observations identify 4.1G as a novel A1R-binding partner that can regulate adenosine action.

Original languageEnglish (US)
Pages (from-to)51-59
Number of pages9
JournalBiochemical Journal
Volume377
Issue number1
DOIs
StatePublished - Jan 1 2004

Keywords

  • Intracellular calcium release
  • Protein-binding partner
  • Yeast two-hybrid
  • cAMP accumulation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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