AustralieFrV1, PascalFrancis, Corpus, bibRecord, 004406

The BAR domain proteins : Molding membranes in fission, fusion, and phagy

Identifieur interne : 004406 ( PascalFrancis/Corpus ); précédent : 004405; suivant : 004407

The BAR domain proteins : Molding membranes in fission, fusion, and phagy

Auteurs : GANG REN ; Parimala Vajjhala ; Janet S. Lee ; Barbara Winsor ; Alan L. Munn

Source :

Microbiology and molecular biology reviews [ 1092-2172 ] ; 2006.

RBID : Pascal:06-0257242

Descripteurs français

Pascal (Inist)
- Protéine membranaire, Protéine fusion, Article synthèse.

English descriptors

KwdEn :
- Fusion protein, Membrane protein, Review.

Abstract

The Binl/amphiphysin/Rvsl67 (BAR) domain proteins are a ubiquitous protein family. Genes encoding members of this family have not yet been found in the genomes of prokaryotes, but within eukaryotes, BAR domain proteins are found universally from unicellular eukaryotes such as yeast through to plants, insects, and vertebrates. BAR domain proteins share an N-terminal BAR domain with a high propensity to adopt α-helical structure and engage in coiled-coil interactions with other proteins. BAR domain proteins are implicated in processes as fundamental and diverse as fission of synaptic vesicles, cell polarity, endocytosis, regulation of the actin cytoskeleton, transcriptional repression, cell-cell fusion, signal transduction, apoptosis, secretory vesicle fusion, excitation-contraction coupling, learning and memory, tissue differentiation, ion flux across membranes, and tumor suppression. What has been lacking is a molecular understanding of the role of the BAR domain protein in each process. The three-dimensional structure of the BAR domain has now been determined and valuable insight has been gained in understanding the interactions of BAR domains with membranes. The cellular roles of BAR domain proteins, characterized over the past decade in cells as distinct as yeasts, neurons, and myocytes, can now be understood in terms of a fundamental molecular function of all BAR domain proteins: to sense membrane curvature, to bind GTPases, and to mold a diversity of cellular membranes.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

A01	`01`	`1`		`@0 1092-2172`
A02	`01`			`@0 MMBRF7`
A03		`1`		`@0 Microbiol. mol. biol. rev.`
A05				`@2 70`
A06				`@2 1`
A08	`01`	`1`	`ENG`	`@1 The BAR domain proteins : Molding membranes in fission, fusion, and phagy`
A11	`01`	`1`		`@1 GANG REN`
A11	`02`	`1`		`@1 VAJJHALA (Parimala)`
A11	`03`	`1`		`@1 LEE (Janet S.)`
A11	`04`	`1`		`@1 WINSOR (Barbara)`
A11	`05`	`1`		`@1 MUNN (Alan L.)`
A14	`01`			`@1 Institute for Molecular Bioscience, University of Queensland @2 St. Lucia, Queensland 4072 @3 AUS @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 5 aut.`
A14	`02`			`@1 UMR7156, Centre National Recherche Scientifique, Université Louis Pasteur @2 Strasbourg 67084 @3 FRA @Z 1 aut. @Z 4 aut.`
A14	`03`			`@1 ARC Special Research Centre for Functional and Applied Genomics, University of Queensland @2 St. Lucia, Queensland 4072 @3 AUS @Z 5 aut.`
A14	`04`			`@1 School of Biomedical Sciences, University of Queensland @2 St. Lucia, Queensland 4072 @3 AUS @Z 5 aut.`
A20				`@2 37-120, a-b [86 p.]`
A21				`@1 2006`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 2044A @5 354000153441390020`
A44				`@0 0000 @1 © 2006 INIST-CNRS. All rights reserved.`
A45				`@0 390 ref.`
A47	`01`	`1`		`@0 06-0257242`
A60				`@1 P`
A61				`@0 A`
A64	`01`	`1`		`@0 Microbiology and molecular biology reviews`
A66	`01`			`@0 USA`
C01	`01`		`ENG`	@0 The Binl/amphiphysin/Rvsl67 (BAR) domain proteins are a ubiquitous protein family. Genes encoding members of this family have not yet been found in the genomes of prokaryotes, but within eukaryotes, BAR domain proteins are found universally from unicellular eukaryotes such as yeast through to plants, insects, and vertebrates. BAR domain proteins share an N-terminal BAR domain with a high propensity to adopt α-helical structure and engage in coiled-coil interactions with other proteins. BAR domain proteins are implicated in processes as fundamental and diverse as fission of synaptic vesicles, cell polarity, endocytosis, regulation of the actin cytoskeleton, transcriptional repression, cell-cell fusion, signal transduction, apoptosis, secretory vesicle fusion, excitation-contraction coupling, learning and memory, tissue differentiation, ion flux across membranes, and tumor suppression. What has been lacking is a molecular understanding of the role of the BAR domain protein in each process. The three-dimensional structure of the BAR domain has now been determined and valuable insight has been gained in understanding the interactions of BAR domains with membranes. The cellular roles of BAR domain proteins, characterized over the past decade in cells as distinct as yeasts, neurons, and myocytes, can now be understood in terms of a fundamental molecular function of all BAR domain proteins: to sense membrane curvature, to bind GTPases, and to mold a diversity of cellular membranes.
C02	`01`	`X`		`@0 002A05`
C03	`01`	`X`	`FRE`	`@0 Protéine membranaire @5 05`
C03	`01`	`X`	`ENG`	`@0 Membrane protein @5 05`
C03	`01`	`X`	`SPA`	`@0 Proteína membranar @5 05`
C03	`02`	`X`	`FRE`	`@0 Protéine fusion @5 06`
C03	`02`	`X`	`ENG`	`@0 Fusion protein @5 06`
C03	`02`	`X`	`SPA`	`@0 Proteína fusionada @5 06`
C03	`03`	`X`	`FRE`	`@0 Article synthèse @5 07`
C03	`03`	`X`	`ENG`	`@0 Review @5 07`
C03	`03`	`X`	`SPA`	`@0 Artículo síntesis @5 07`
N21				`@1 163`
N44	`01`			`@1 OTO`
N82				`@1 OTO`

Format Inist (serveur)

NO :	PASCAL 06-0257242 INIST
ET :	The BAR domain proteins : Molding membranes in fission, fusion, and phagy
AU :	GANG REN; VAJJHALA (Parimala); LEE (Janet S.); WINSOR (Barbara); MUNN (Alan L.)
AF :	Institute for Molecular Bioscience, University of Queensland/St. Lucia, Queensland 4072/Australie (1 aut., 2 aut., 3 aut., 5 aut.); UMR7156, Centre National Recherche Scientifique, Université Louis Pasteur/Strasbourg 67084/France (1 aut., 4 aut.); ARC Special Research Centre for Functional and Applied Genomics, University of Queensland/St. Lucia, Queensland 4072/Australie (5 aut.); School of Biomedical Sciences, University of Queensland/St. Lucia, Queensland 4072/Australie (5 aut.)
DT :	Publication en série; Niveau analytique
SO :	Microbiology and molecular biology reviews; ISSN 1092-2172; Coden MMBRF7; Etats-Unis; Da. 2006; Vol. 70; No. 1; 37-120, a-b [86 p.]; Bibl. 390 ref.
LA :	Anglais
EA :	The Binl/amphiphysin/Rvsl67 (BAR) domain proteins are a ubiquitous protein family. Genes encoding members of this family have not yet been found in the genomes of prokaryotes, but within eukaryotes, BAR domain proteins are found universally from unicellular eukaryotes such as yeast through to plants, insects, and vertebrates. BAR domain proteins share an N-terminal BAR domain with a high propensity to adopt α-helical structure and engage in coiled-coil interactions with other proteins. BAR domain proteins are implicated in processes as fundamental and diverse as fission of synaptic vesicles, cell polarity, endocytosis, regulation of the actin cytoskeleton, transcriptional repression, cell-cell fusion, signal transduction, apoptosis, secretory vesicle fusion, excitation-contraction coupling, learning and memory, tissue differentiation, ion flux across membranes, and tumor suppression. What has been lacking is a molecular understanding of the role of the BAR domain protein in each process. The three-dimensional structure of the BAR domain has now been determined and valuable insight has been gained in understanding the interactions of BAR domains with membranes. The cellular roles of BAR domain proteins, characterized over the past decade in cells as distinct as yeasts, neurons, and myocytes, can now be understood in terms of a fundamental molecular function of all BAR domain proteins: to sense membrane curvature, to bind GTPases, and to mold a diversity of cellular membranes.
CC :	002A05
FD :	Protéine membranaire; Protéine fusion; Article synthèse
ED :	Membrane protein; Fusion protein; Review
SD :	Proteína membranar; Proteína fusionada; Artículo síntesis
LO :	INIST-2044A.354000153441390020
ID :	06-0257242

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Pascal:06-0257242

Le document en format XML

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<front><div type="abstract" xml:lang="en">The Binl/amphiphysin/Rvsl67 (BAR) domain proteins are a ubiquitous protein family. Genes encoding members of this family have not yet been found in the genomes of prokaryotes, but within eukaryotes, BAR domain proteins are found universally from unicellular eukaryotes such as yeast through to plants, insects, and vertebrates. BAR domain proteins share an N-terminal BAR domain with a high propensity to adopt α-helical structure and engage in coiled-coil interactions with other proteins. BAR domain proteins are implicated in processes as fundamental and diverse as fission of synaptic vesicles, cell polarity, endocytosis, regulation of the actin cytoskeleton, transcriptional repression, cell-cell fusion, signal transduction, apoptosis, secretory vesicle fusion, excitation-contraction coupling, learning and memory, tissue differentiation, ion flux across membranes, and tumor suppression. What has been lacking is a molecular understanding of the role of the BAR domain protein in each process. The three-dimensional structure of the BAR domain has now been determined and valuable insight has been gained in understanding the interactions of BAR domains with membranes. The cellular roles of BAR domain proteins, characterized over the past decade in cells as distinct as yeasts, neurons, and myocytes, can now be understood in terms of a fundamental molecular function of all BAR domain proteins: to sense membrane curvature, to bind GTPases, and to mold a diversity of cellular membranes.</div>
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<AF>Institute for Molecular Bioscience, University of Queensland/St. Lucia, Queensland 4072/Australie (1 aut., 2 aut., 3 aut., 5 aut.); UMR7156, Centre National Recherche Scientifique, Université Louis Pasteur/Strasbourg 67084/France (1 aut., 4 aut.); ARC Special Research Centre for Functional and Applied Genomics, University of Queensland/St. Lucia, Queensland 4072/Australie (5 aut.); School of Biomedical Sciences, University of Queensland/St. Lucia, Queensland 4072/Australie (5 aut.)</AF>
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<SO>Microbiology and molecular biology reviews; ISSN 1092-2172; Coden MMBRF7; Etats-Unis; Da. 2006; Vol. 70; No. 1; 37-120, a-b [86 p.]; Bibl. 390 ref.</SO>
<LA>Anglais</LA>
<EA>The Binl/amphiphysin/Rvsl67 (BAR) domain proteins are a ubiquitous protein family. Genes encoding members of this family have not yet been found in the genomes of prokaryotes, but within eukaryotes, BAR domain proteins are found universally from unicellular eukaryotes such as yeast through to plants, insects, and vertebrates. BAR domain proteins share an N-terminal BAR domain with a high propensity to adopt α-helical structure and engage in coiled-coil interactions with other proteins. BAR domain proteins are implicated in processes as fundamental and diverse as fission of synaptic vesicles, cell polarity, endocytosis, regulation of the actin cytoskeleton, transcriptional repression, cell-cell fusion, signal transduction, apoptosis, secretory vesicle fusion, excitation-contraction coupling, learning and memory, tissue differentiation, ion flux across membranes, and tumor suppression. What has been lacking is a molecular understanding of the role of the BAR domain protein in each process. The three-dimensional structure of the BAR domain has now been determined and valuable insight has been gained in understanding the interactions of BAR domains with membranes. The cellular roles of BAR domain proteins, characterized over the past decade in cells as distinct as yeasts, neurons, and myocytes, can now be understood in terms of a fundamental molecular function of all BAR domain proteins: to sense membrane curvature, to bind GTPases, and to mold a diversity of cellular membranes.</EA>
<CC>002A05</CC>
<FD>Protéine membranaire; Protéine fusion; Article synthèse</FD>
<ED>Membrane protein; Fusion protein; Review</ED>
<SD>Proteína membranar; Proteína fusionada; Artículo síntesis</SD>
<LO>INIST-2044A.354000153441390020</LO>
<ID>06-0257242</ID>
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The BAR domain proteins : Molding membranes in fission, fusion, and phagy

The BAR domain proteins : Molding membranes in fission, fusion, and phagy

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