Asp3Gly polymorphism affects fatty acid‐binding protein 3 intracellular stability and subcellular localization. Issue 18 (20th July 2015)

• Record Type: Journal Article
• Authors: Kusudo, Tatsuya; Hashida, Yasuhiko; Ando, Fujiko; Shimokata, Hiroshi; Yamashita, Hitoshi
• Is Part Of: FEBS letters. Volume 589:Issue 18(2015)
• Page Start: 2382
• Page End: 2387
• Publication Date: 2015-07-20
• Subjects: Fatty acid binding protein -- Polymorphism -- Single-nucleotide polymorphism -- Protein stability -- Subcellular localizatoin; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2015.07.007
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Fatty acid‐binding proteins (FABP) play a crucial role in intracellular fatty acid transportation and metabolism. In this study, we investigate the effects of the FABP3 Asp3Gly (D3G) polymorphism on protein structure and function. Although the mutation did not alter protein secondary structure or the ability to bind 1‐anilinonaphthalene‐8‐sulfonic acid and palmitate, the intracellular stability of the D3G mutant was significantly decreased. Immunocytochemical analysis reveals that the mutation alters FABP3 subcellular localization. Our results suggest that the D3G polymorphism may impact energy metabolism and physiological functions. Abstract : The effects of the FABP3 Asp3Gly polymorphism on protein structure and function were investigated. The Asp3Gly mutation decreases FABP3 intracellular stability. The Asp3Gly mutation also influences FABP3 subcellular localization.