The majority of cellular fatty acid acylated proteins are localized to the cytoplasmic surface of the plasma membrane

Wilcox, Celeste A.; Olson, Eric N.

doi:10.1021/bi00378a008

Cited by 45 publications

(11 citation statements)

References 41 publications

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“…GLUT1 has six cysteine residues, several of which are predicted to have access to the cytoplasmic compartment (33). This localization favors palmitoylation (60). Indeed, Pouliot and Beliveau (38) have demonstrated that GLUT1 in brain capillaries is palmitoylated.…”

Section: Discussionmentioning

confidence: 99%

Glucose deprivation enhances targeting of GLUT1 to lipid rafts in 3T3-L1 adipocytes

Kumar

Xiao

Laipis

et al. 2004

American Journal of Physiology-Endocrinology and Metabolism

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. Glucose deprivation enhances targeting of GLUT1 to lipid rafts in 3T3-L1 adipocytes. Am J Physiol Endocrinol Metab 286: E568-E576, 2004. First published December 9, 2003 10.1152/ajpendo.00372.2003.-Glucose deprivation dramatically increases glucose transport activity in 3T3-L1 adipocytes without changing the concentration of GLUT1 in the plasma membrane (PM). Recent data suggest that subcompartments within the PM, specifically lipid rafts, may sequester selected proteins and alter their activity. To evaluate this possibility, we examined the distribution of GLUT1 in Triton X-100-soluble and -insoluble fractions. Our data show that 77% of the GLUT1 pool in PMs isolated from control 3T3-L1 adipocytes was extracted by 0.2% Triton X-100. After glucose deprivation for 12 h, only 56% of GLUT1 was extracted by detergent. In contrast, there was a twofold increase in the GLUT1 content of the detergent-resistant fraction. To evaluate whether GLUT1 interacts with a specific protein within lipid rafts, we focused on stomatin, recently shown to interact with and inhibit GLUT1 activity. Stomatin is distributed about equally between the PM and the biosynthetic compartments, and its expression is not affected by glucose deprivation. Nearly 90% of the PM pool of stomatin is in detergent-resistant lipid rafts. In normal 3T3-L1 adipocytes, we were unable to demonstrate an interaction between GLUT1 and stomatin in coimmunoprecipitation experiments. However, in stomatin-overexpressing cells, there was clear coprecipitation of stomatin with GLUT1 antibodies. Glucose deprivation increased this interaction threefold, which may reflect the increase of GLUT1 in lipid rafts. Despite this, there was little change in transport activity in glucosedeprived, stomatin-overexpressing cells vs. that in control cells. Thus GLUT1 interacts with stomatin in lipid rafts, but this interaction per se does not alter transport activity. Rather, stomatin may serve as an anchor for GLUT1 in lipid rafts, the environment of which favors activation.glucose transporter 1; lipid rafts; stomatin MOST CELLS ARE DEPENDENT ON GLUCOSE UPTAKE and metabolism as a source of energy. Although the number of members of the transporter family is expanding, GLUT1 is ubiquitously expressed and is responsible for constitutive uptake in mammalian cells. The regulation of GLUT1 expression and activity has been intensively studied. Our focus has been on the nutrient-dependent regulation of glucose transport in 3T3-L1 adipocytes. Specifically, we (and others) have shown that a decrease in extracellular glucose concentration increases transport activity in 3T3-L1 adipocytes in a protein synthesisdependent fashion (27,39,55,56). Although complete glucose deprivation increases transport activity 10-to 15-fold, a change of fourfold is observed within the range of 2.5 to 25 mM, the limits of circulating glucose concentration in diabetic patients, suggesting physiological relevance. Although 3T3-L1 adipocytes express both GLUT1 and GLUT4, the insulin-stimulated transporter, the effec...

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Section: Discussionmentioning

confidence: 99%

Glucose deprivation enhances targeting of GLUT1 to lipid rafts in 3T3-L1 adipocytes

Kumar

Xiao

Laipis

et al. 2004

American Journal of Physiology-Endocrinology and Metabolism

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“…First, the native structure of FABP may possess a more appropriate conformational state for easy binding to its putative receptor. It has been shown that platelet-derived CD36 is part of the signal-transduction system associated with c-src oncogene family kinases [15] that play a role in the control of cell growth [27]. It is interesting to note that recently Yang et al [33] demonstrated that recombinant, rat intestine FABP and bovine liver type FABP, did not inhibit the growth of mouse epithelial cells, as did mammary-derived growth inhibitor (MDGI) FABP or bovine heart FABP.…”

Section: Detection Of Fabp-cd36 Complexes By Immunoprecipitation and mentioning

confidence: 99%

Association and Coexpression of Fatty-Acid-Binding Protein and Glycoprotein CD36 in the Bovine Mammary Gland

Spitsberg¹,

Matitashvili²,

Gorewit³

1995

Eur J Biochem

168

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The involvement of glycoprotein CD36 and fatty-acid-binding protein (FABP) in cellular growth, differentiation, lipid transport and metabolism led us to examine the possible biochemical and physiological relationship(s) between these two proteins. We investigated three aspects of this relationship. We first attempted to identify any physical complex formed between CD36 and FABP in bovine milk fat globule membranes. These membranes are the product of mammary gland secretory epithelial cells. The second aspect studied was the effect of synthetic peptide analogs to the C-terminus (amino acid residues 121-131) of bovine mammary gland FABP on cell proliferation, as a result of the interaction of these peptides with the ectodomain of CD36. Finally, mammary gland CD36 and FABP coexpression was defined at different stages of lactation and during involution. Immunoprecipitation, Western immunoblotting with anti-FABP and anti-CD36, Northern-blot analysis and a mammary epithelial cell proliferation assay demonstrated that: (a) bovine milk fat globule membranes contain the complex of CD36 and FABP, and that this complex is, most likely, formed as a result of FABP binding to the cytoplasmic segments of CD36; (b) synthetic analog of the C-terminus of FABP with the sequence Val-Thr-Cys, identical to the sequence found in the CD36-binding domain of thrombospondin, was a more potent inhibitor of bovine mammary gland epithelial cell proliferation than a synthetic peptide with the Val-Cys-Thr sequence; (c) the expression of FABP and CD36 is related to the state of mammary cell differentiation, since it reaches its maximum during lactation and declines during the involutionary period.

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“…Golgi and plasma membranes were isolated by sucrose gradient centrifugation (33), and the identity and purity of these membrane populations were determined by enzyme markers. Alkaline phosphatase and P-1,3-galactosyltransferase have been reported to be plasma membrane and Golgi membrane markers, respectively, consistent with results of this study.…”

Section: Figmentioning

confidence: 99%

Cell surface and Golgi pools of beta-1,4-galactosyltransferase are differentially regulated during embryonal carcinoma cell differentiation.

Lopez¹,

Maillet²,

Oleszkowicz³

et al. 1989

Mol. Cell. Biol.

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beta-1,4-Galactosyltransferase (GalTase) has two functionally distinct subcellular distributions. In the Golgi apparatus, GalTase participates in the glycosylation of secretory and membrane-bound glycoproteins, whereas on the cell surface it mediates specific aspects of intercellular adhesion. For this study, a murine GalTase clone was obtained by screening a lambda gt10 cDNA library made from F9 embryonal carcinoma cells with a heterologous bovine GalTase cDNA probe. The murine GalTase cDNA probe was used in conjunction with assays of GalTase activity to investigate the expression and distribution of GalTase during differentiation of F9 stem cells into secretory endodermal epithelium. During the initial phase of F9 cell differentiation, GalTase mRNA levels remained relatively constant; however, as differentiation progressed, as assayed by expression of the differentiation-specific marker laminin B1, GalTase mRNA levels and enzyme activity rose dramatically. Furthermore, subcellular fractionation of these cells showed that the increased GalTase levels were specifically associated with the Golgi apparatus, whereas GalTase specific activity on the plasma membrane remained constant. These results show that levels of cell surface and Golgi GalTase change relative to one another during F9 cell differentiation and suggest that these functionally distinct pools of GalTase are independently and differentially regulated.

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The majority of cellular fatty acid acylated proteins are localized to the cytoplasmic surface of the plasma membrane

Cited by 45 publications

References 41 publications

Glucose deprivation enhances targeting of GLUT1 to lipid rafts in 3T3-L1 adipocytes

Glucose deprivation enhances targeting of GLUT1 to lipid rafts in 3T3-L1 adipocytes

Association and Coexpression of Fatty-Acid-Binding Protein and Glycoprotein CD36 in the Bovine Mammary Gland

Cell surface and Golgi pools of beta-1,4-galactosyltransferase are differentially regulated during embryonal carcinoma cell differentiation.

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