[Proteins sharing PNPLA domain, a new family of enzymes regulating lipid metabolism]

Med Sci (Paris). 2010 Feb;26(2):177-84. doi: 10.1051/medsci/2010262177.
[Article in French]

Abstract

Genome sequencing technologies led to tremendous breakthrough in biology uncovering numerous genes unknown so far and thus opening the field of deep investigations to understand their associated biological functions. As a matter of fact, functional genomics have been progressively replacing sequence genomics with as a main objective to yield insight into cellular physiology. Recently, an emerging group of genes coding for proteins bearing a common domain termed patatin (PNPLA domain) have been discovered. Members of this new enzymatic family displaying lipase and transacylase properties appeared to have major roles in the regulation of lipid metabolism. The aim of this review is to make an overview on the latest discoveries concerning this new family of proteins and their relationship with lipid metabolism, physiology of mammals and their potential involvement in human pathology.

Publication types

  • Comparative Study
  • English Abstract
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arabidopsis Proteins / chemistry
  • Arabidopsis Proteins / physiology
  • Caenorhabditis elegans Proteins / chemistry
  • Caenorhabditis elegans Proteins / physiology
  • Carboxylic Ester Hydrolases / chemistry
  • Carboxylic Ester Hydrolases / classification
  • Carboxylic Ester Hydrolases / genetics
  • Carboxylic Ester Hydrolases / physiology*
  • Catalytic Domain* / genetics
  • Conserved Sequence
  • Drosophila Proteins / chemistry
  • Drosophila Proteins / physiology
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / physiology*
  • Humans
  • Lipase / chemistry
  • Lipase / physiology
  • Lipid Metabolism / genetics
  • Lipid Metabolism / physiology*
  • Lipolysis / genetics*
  • Mammals / metabolism
  • Mice
  • Molecular Sequence Data
  • Multigene Family*
  • Phospholipases A2, Calcium-Independent / chemistry
  • Phospholipases A2, Calcium-Independent / physiology
  • Phylogeny
  • Plant Proteins / chemistry
  • Plant Proteins / physiology
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / physiology
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Species Specificity

Substances

  • Arabidopsis Proteins
  • Caenorhabditis elegans Proteins
  • Drosophila Proteins
  • Escherichia coli Proteins
  • Plant Proteins
  • Saccharomyces cerevisiae Proteins
  • patatin protein, Solanum tuberosum
  • Carboxylic Ester Hydrolases
  • Lipase
  • PNPLA1 protein, human
  • PNPLA2 protein, human
  • PNPLA4 protein, human
  • PNPLA5 protein, human
  • Phospholipases A2, Calcium-Independent