Glycerol facilitator of Escherichia coli: cloning of glpF and identification of the glpF product

Sweet, Gaye; Gandor, Christine R.; Voegele, Ralf T.; Wittekindt, Nicola E.; Beuerle, Joachim; Truniger, Verónica; Lin, E. C. C.; Boos, Winfried

doi:10.1128/jb.172.1.424-430.1990

Cited by 145 publications

(113 citation statements)

References 40 publications

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“…Sweet and coworkers (32) showed that GlpF is an aquaglyceroporin prototype in Escherichia coli (32). Aquaglyceroporins facilitate glycerol transport according to glycerol gradient.…”

Section: Discussionmentioning

confidence: 99%

Adaptation to fasting by glycerol transport through aquaporin 7 in adipose tissue

Maeda

Funahashi

Hibuse

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

162

134

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Adipocytes hydrolyze triglycerides and secrete free fatty acids and glycerol into the circulation. The molecular mechanism involved in glycerol transport from adipocytes has not been elucidated. Here, we investigated glycerol and glucose metabolism in mice lacking aquaporin 7 (Aqp7), a member of the aquaglyceroporins expressed in adipose tissue, and demonstrated that Aqp7 functions as a glycerol gateway molecule in vivo. Aqp7-knockout (KO) mice had lower plasma glycerol levels compared with WT mice but had normal plasma free fatty acid levels. The increase in plasma glycerol level in response to ␤3-adrenergic agonist was severely impaired in KO mice. Epinephrine-stimulated glycerol secretion was also impaired in Aqp7 knockdown adipocytes. During prolonged fasting, plasma glycerol was elevated and the plasma glucose level was maintained in WT mice. In contrast, KO mice showed a disrupted increase of plasma glycerol and rapid reduction of plasma glucose during prolonged fasting. Our findings indicate that the lack of effective glycerol transport from adipocytes by glycerol gateway molecule causes defective adaptation to prolonged fasting.adipocyte ͉ gluconeogenesis ͉ lipolysis ͉ knockout mice

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“…Sweet and coworkers (32) showed that GlpF is an aquaglyceroporin prototype in Escherichia coli (32). Aquaglyceroporins facilitate glycerol transport according to glycerol gradient.…”

Section: Discussionmentioning

confidence: 99%

Adaptation to fasting by glycerol transport through aquaporin 7 in adipose tissue

Maeda

Funahashi

Hibuse

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

162

134

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“…Furthermore GUP1 and GUP2 have recently been proposed to be involved in active transport of glycerol in yeasts (13). In contrast, the physiologically relevant role of GlpF from Escherichia coli, the closest bacterial homolog of Fps1p with 30.5% identity, is likely to be import of glycerol for catabolism (14,15).…”

Section: Major Intrinsic Protein (Mip)mentioning

confidence: 99%

Analysis of the Pore of the Unusual Major Intrinsic Protein Channel, Yeast Fps1p

Bill

Hedfalk

Karlgren

et al. 2001

Journal of Biological Chemistry

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Fps1p is a glycerol efflux channel from Saccharomyces cerevisiae. In this atypical major intrinsic protein neither of the signature NPA motifs of the family, which are part of the pore, is preserved. To understand the functional consequences of this feature, we analyzed the pseudo-NPA motifs of Fps1p by site-directed mutagenesis and assayed the resultant mutant proteins in vivo. In addition, we took advantage of the fact that the closest bacterial homolog of Fps1p, Escherichia coli GlpF, can be functionally expressed in yeast, thus enabling the analysis in yeast cells of mutations that make this typical major intrinsic protein more similar to Fps1p. We observed that mutations made in Fps1p to "restore" the signature NPA motifs did not substantially affect channel function. In contrast, when GlpF was mutated to resemble Fps1p, all mutants had reduced activity compared with wild type. We rationalized these data by constructing models of one GlpF mutant and of the transmembrane core of Fps1p. Our model predicts that the pore of Fps1p is more flexible than that of GlpF. We discuss the fact that this may accommodate the divergent NPA motifs of Fps1p and that the different pore structures of Fps1p and GlpF may reflect the physiological roles of the two glycerol facilitators.

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“…The best-known example of this type of uniport is the glycerol facilitator (GlpF) of E. coli [29]. Glycerol uptake is followed by glycerol kinase catalyzed conversion to sn-glycerol 3-phosphate [30].…”

Section: Ii-b Electroneutral Solute Uniport (Fig 1-1)mentioning

confidence: 99%

Secondary solute transport in bacteria

Poolman

Konings

1993

Biochimica et Biophysica Acta (BBA) - Bioenergetics

202

160

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Glycerol facilitator of Escherichia coli: cloning of glpF and identification of the glpF product

Cited by 145 publications

References 40 publications

Adaptation to fasting by glycerol transport through aquaporin 7 in adipose tissue

Adaptation to fasting by glycerol transport through aquaporin 7 in adipose tissue

Analysis of the Pore of the Unusual Major Intrinsic Protein Channel, Yeast Fps1p

Secondary solute transport in bacteria

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