Disruption of the Saccharomyces cerevisiae Homologue to the Murine Fatty Acid Transport Protein Impairs Uptake and Growth on Long-chain Fatty Acids

Færgeman, Nils J.; DiRusso, Concetta C.; Elberger, Andrea J.; Knudsen, Jens; Black, Paul N.

doi:10.1074/jbc.272.13.8531

Cited by 159 publications

(172 citation statements)

References 48 publications

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“…S3). 18 Furthermore, the gpt2D, ayr1D and An exposure of WT cells to various concentrations of exogenous POA elicits differential effects on the relative levels of C 16:1 molecular species (i.e., POA-containing species) of all major classes of PL, and the atg32D-dependent mutational block of mitophagy alters these effects. WT and atg32D cells were recovered at days 1, 2 and 4 of culturing in YP medium initially containing 0.2% glucose as carbon source.…”

Section: -15mentioning

confidence: 99%

“…1 To further verify our hypothesis, we examined how various single-gene-deletion mutations (each eliminating an enzyme involved in POA transport to the ER or in POA incorporation into PL and/or NL within the ER; see refs. [7][8][9][10][11][12][13][14][15][16][17][18] and Fig. S3) influence the susceptibility of yeast to POA-induced liponecrotic PCD.…”

Section: -15mentioning

confidence: 99%

“…S3). [7][8][9][10][11][12][13][14][15][16][17][18] It is conceivable therefore that: (1) POA-containing species of PA, PS, PE, PC and PI could amass within the PM bilayer of yeast treated with POA; and (2) such buildup of POA-containing species of PL within the PM could alter the proper PL asymmetry in the PM bilayer and, thus, could induce the alkaline-pH-and lipid-asymmetryresponsive Rim101 signaling pathway.…”

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confidence: 99%

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Mechanism of liponecrosis, a distinct mode of programmed cell death

Richard¹,

Beach²,

Piano³

et al. 2014

Cell Cycle

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Section: -15mentioning

confidence: 99%

Section: -15mentioning

confidence: 99%

mentioning

confidence: 99%

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Mechanism of liponecrosis, a distinct mode of programmed cell death

Richard¹,

Beach²,

Piano³

et al. 2014

Cell Cycle

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“…A transgenic mouse model with cardiac-specific expression of FATP1 demonstrated increased myocardial LCFA uptake (13). Disruption of the FATP1 homolog expressed in yeast, fat1p, markedly impaired LCFA uptake (14), and a murine FATP1 knockout mouse exhibited reduced muscle acyl-CoA levels and increased insulin sensitivity (15).…”

mentioning

confidence: 99%

Fatty acid metabolism in adipocytes: functional analysis of fatty acid transport proteins 1 and 4

Lobo

Wiczer

Smith

et al. 2007

Journal of Lipid Research

132

116

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The role of fatty acid transport protein 1 (FATP1) and FATP4 in facilitating adipocyte fatty acid metabolism was investigated using stable FATP1 or FATP4 knockdown (kd) 3T3-L1 cell lines derived from retrovirus-delivered short hairpin RNA (shRNA). Decreased expression of FATP1 or FATP4 did not affect preadipocyte differentiation or the expression of FATP1 (in FATP4 kd), FATP4 (in FATP1 kd), fatty acid translocase, acyl-coenzyme A synthetase 1, and adipocyte fatty acid binding protein but did lead to increased levels of peroxisome proliferator-activated receptor g and CCAAT/enhancer binding protein a. Both FATP1 and FATP4 kd adipocytes exhibited reduced triacylglycerol deposition and corresponding reductions in diacylglycerol and monoacylglycerol levels compared with control cells. FATP1 kd adipocytes displayed an ?25% reduction in basal 3 H-labeled fatty acid uptake and a complete loss of insulin-stimulated 3 H-labeled fatty acid uptake compared with control adipocytes. In contrast, FATP4 kd adipocytes as well as HEK-293 cells overexpressing FATP4 did not display any changes in fatty acid influx. FATP4 kd cells exhibited increased basal lipolysis, whereas FATP1 kd cells exhibited no change in lipolytic capacity. Consistent with reduced triacylglycerol accumulation, FATP1 and FATP4 kd adipocytes exhibited enhanced 2-deoxyglucose uptake compared with control adipocytes. These findings define unique and distinct roles for FATP1 and FATP4 in adipose fatty acid metabolism.

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“…In mammalian cells, FATP isoforms 1-6 have been identified based on sequence similarity and have distinct tissue-specific distributions of expression (9). The yeast homologue (Fat1p) has been shown by genetic and biochemical analyses to be required for fatty acid uptake (10).…”

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confidence: 99%

Characterization of the Acyl-CoA Synthetase Activity of Purified Murine Fatty Acid Transport Protein 1

Hall

Smith

Bernlohr

2003

Journal of Biological Chemistry

153

118

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Fatty acid transport protein 1 (FATP1) is an ϳ63-kDa plasma membrane protein that facilitates the influx of fatty acids into adipocytes as well as skeletal and cardiac myocytes. Previous studies with FATP1 expressed in COS1 cell extracts suggested that FATP1 exhibits very long chain acyl-CoA synthetase (ACS) activity and that such activity may be linked to fatty acid transport. To address the enzymatic activity of the isolated protein, murine FATP1 and ACS1 were engineered to contain a C-terminal Myc-His tag expressed in COS1 cells via adenoviral-mediated infection and purified to homogeneity using nickel affinity chromatography. Kinetic analysis of the purified enzymes was carried out for long chain palmitic acid (C16:0) and very long chain lignoceric acid (C24:0) as well as for ATP and CoA. FATP1 exhibited similar substrate specificity for fatty acids 16 -24 carbons in length, whereas ACS1 was 10-fold more active on long chain fatty acids relative to very long chain fatty acids. The very long chain acyl-CoA synthetase activity of the two enzymes was comparable as were the K m values for both ATP and coenzyme A. Interestingly, FATP1 was insensitive to inhibition by triacsin C, whereas ACS1 was inhibited by micromolar concentrations of the compound. These data represent the first characterization of purified FATP1 and indicate that the enzyme is a broad substrate specificity acyl-CoA synthetase. These findings are consistent with the hypothesis that that fatty acid uptake into cells is linked to their esterification with coenzyme A.

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Disruption of the Saccharomyces cerevisiae Homologue to the Murine Fatty Acid Transport Protein Impairs Uptake and Growth on Long-chain Fatty Acids

Cited by 159 publications

References 48 publications

Mechanism of liponecrosis, a distinct mode of programmed cell death

Mechanism of liponecrosis, a distinct mode of programmed cell death

Fatty acid metabolism in adipocytes: functional analysis of fatty acid transport proteins 1 and 4

Characterization of the Acyl-CoA Synthetase Activity of Purified Murine Fatty Acid Transport Protein 1

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