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Fatty acid transport protein chimeras define functional domains
Author(s) -
Darwis Dina A.,
Quackenbush Steve,
DiRusso Concetta,
Black Paul
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a82-c
Subject(s) - gene isoform , fatty acid , biochemistry , biology , transport protein , microbiology and biotechnology , gene
Fatty acids are involved in essential metabolic processes including production of metabolic energy and providing precursors for membrane lipid biosynthesis. Several membrane proteins have been proposed to facilitate cellular fatty acid uptake. Amongst these is the fatty acid transport protein (FATPs) family, which consists of six isoforms (FATP1‐6) that have distinct expression patterns and intrinsic acyl Co‐A synthetase activity. The precise role(s) of the different FATP isoforms in mediating fatty acid transport and trafficking are not well defined. Our laboratory recently characterized the murine FATP family members expressed in yeast and showed that they have distinct transport and activation activities. We hypothesize regions adjacent to and within the highly conserved ATP/AMP and FATP/VLACS motifs found in the FATP isoforms distinguish their unique transport and activation activities. A series of protein chimeras using the mmFATP1, 4 and 6 isoforms were constructed to test the hypothesis. Results from these experiments showed the fatty acid transport and activation activities within these mmFATP isoforms were distinguishable and were consistent with the notion that elements within and adjacent to the FATP/VLACS motif are crucial for fatty acid transport. This work is supported by NIH grant R01GM56850.