Les multiples fonctions des protéines lipolytiques à domaine patatine

Thierry Heitz

doi:10.1051/medsci/2010262128

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Volume 26 / Numéro 2 (Février 2010)

Med Sci (Paris), 26 2 (2010) 128-130

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Numéro		Med Sci (Paris) Volume 26, Numéro 2, Février 2010


Page(s)		128 - 130
Section		Nouvelles
DOI		https://doi.org/10.1051/medsci/2010262128
Publié en ligne		15 février 2010

Kienesberger PC, Oberer M, Lass A, Zechner R. Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions. J Lipid Res 2009; 50 (suppl) : S63–8. [Google Scholar]
Kershaw EE, Hamm JK, Verhagen LA, et al. Adipose triglyceride lipase: function, regulation by insulin, and comparison with adiponutrin. Diabetes 2006; 55 : 148–57. [Google Scholar]
Zimmermann R, Strauss JG, Haemmerle G, et al. Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase. Science 2004; 306 : 1383–6. [Google Scholar]
Gronke S, Mildner A, Fellert S, et al. Brummer lipase is an evolutionary conserved fat storage regulator in Drosophila. Cell Metab 2005; 1 : 323–30. [Google Scholar]
Kurat CF, Natter K, Petschnigg J, et al. Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast. J Biol Chem 2005; 281 : 491–500. [Google Scholar]
Racusen D, Foote M. A major soluble glycoprotein of potato tubers. J Food Biochem 1980; 4 : 43–52. [Google Scholar]
Eastmond PJ. Sugar-Dependent1 encodes a patatin domain triacylglycerol lipase that initiates storage oil breakdown in germinating Arabidopsis seeds. Plant Cell 2006; 18 : 665–75. [Google Scholar]
Pankhaniya RR, Tamura M, Allmond LR, et al. Pseudomonas aeruginosa causes acute lung injury via the catalytic activity of the patatin-like phospholipase domain of ExoU. Crit Care Med 2004; 32 : 2293–9. [Google Scholar]
Aurass P, Pless B, Rydzewski K, et al. bdhA-patD operon as a virulence determinant, revealed by a novel large-scale approach for identification of Legionella pneumophila mutants defective for amoeba infection. Appl Environ Microbiol 2009; 75 : 4506–15. [Google Scholar]
Banerji S, Flieger A. Patatin-like proteins: a new family of lipolytic enzymes present in bacteria ? Microbiology 2004; 150 : 522–5. [Google Scholar]
La Camera S, Geoffroy P, Samaha H, et al. A pathogen-inducible patatin-like lipid acyl hydrolase facilitates fungal and bacterial host colonization in Arabidopsis. Plant J 2005; 44 : 810–25. [Google Scholar]
La Camera S, Balague C, Göbel C, et al. The Arabidopsis patatin-like protein 2 (PLP2) plays an essential role in cell death execution and differentially affects biosynthesis of oxylipins and resistance to pathogens. Mol Plant Microbe Interact 2009; 2 : 469–81. [Google Scholar]
Baulande S, Langlois C. Les protéines à domaine patatine : une nouvelle famille de régulateurs du métabolisme lipidique. Med Sci (Paris) 2010; 26 : 177–84. [Google Scholar]

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[1] Kienesberger PC, Oberer M, Lass A, Zechner R. Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions. J Lipid Res 2009; 50 (suppl) : S63–8. [Google Scholar]

[2] Kershaw EE, Hamm JK, Verhagen LA, et al. Adipose triglyceride lipase: function, regulation by insulin, and comparison with adiponutrin. Diabetes 2006; 55 : 148–57. [Google Scholar]

[3] Zimmermann R, Strauss JG, Haemmerle G, et al. Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase. Science 2004; 306 : 1383–6. [Google Scholar]

[4] Gronke S, Mildner A, Fellert S, et al. Brummer lipase is an evolutionary conserved fat storage regulator in Drosophila. Cell Metab 2005; 1 : 323–30. [Google Scholar]

[5] Kurat CF, Natter K, Petschnigg J, et al. Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast. J Biol Chem 2005; 281 : 491–500. [Google Scholar]

[6] Racusen D, Foote M. A major soluble glycoprotein of potato tubers. J Food Biochem 1980; 4 : 43–52. [Google Scholar]

[7] Eastmond PJ. Sugar-Dependent1 encodes a patatin domain triacylglycerol lipase that initiates storage oil breakdown in germinating Arabidopsis seeds. Plant Cell 2006; 18 : 665–75. [Google Scholar]

[8] Pankhaniya RR, Tamura M, Allmond LR, et al. Pseudomonas aeruginosa causes acute lung injury via the catalytic activity of the patatin-like phospholipase domain of ExoU. Crit Care Med 2004; 32 : 2293–9. [Google Scholar]

[9] Aurass P, Pless B, Rydzewski K, et al. bdhA-patD operon as a virulence determinant, revealed by a novel large-scale approach for identification of Legionella pneumophila mutants defective for amoeba infection. Appl Environ Microbiol 2009; 75 : 4506–15. [Google Scholar]

[10] Banerji S, Flieger A. Patatin-like proteins: a new family of lipolytic enzymes present in bacteria ? Microbiology 2004; 150 : 522–5. [Google Scholar]

[11] La Camera S, Geoffroy P, Samaha H, et al. A pathogen-inducible patatin-like lipid acyl hydrolase facilitates fungal and bacterial host colonization in Arabidopsis. Plant J 2005; 44 : 810–25. [Google Scholar]

[12] La Camera S, Balague C, Göbel C, et al. The Arabidopsis patatin-like protein 2 (PLP2) plays an essential role in cell death execution and differentially affects biosynthesis of oxylipins and resistance to pathogens. Mol Plant Microbe Interact 2009; 2 : 469–81. [Google Scholar]

[13] Baulande S, Langlois C. Les protéines à domaine patatine : une nouvelle famille de régulateurs du métabolisme lipidique. Med Sci (Paris) 2010; 26 : 177–84. [Google Scholar]