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

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...

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Published inM.S. Médecine sciences Vol. 26; no. 2; p. 177
Main Authors Baulande, Sylvain, Langlois, Clotilde
Format Journal Article
LanguageFrench
Published France 01.02.2010
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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.
AbstractList 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.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.
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.
Author Baulande, Sylvain
Langlois, Clotilde
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SubjectTerms 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
Title Proteins sharing PNPLA domain, a new family of enzymes regulating lipid metabolism
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Volume 26
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