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Barfly: Sculpting membranes at the Drosophila neuromuscular junction

Research output: Contribution to Journal/Magazine › Review article › peer-review

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Barfly: Sculpting membranes at the Drosophila neuromuscular junction. / Oh, Eugene; Robinson, Iain.
In: Developmental Neurobiology, Vol. 72, No. 1, 01.2012, p. 33-56.

Research output: Contribution to Journal/Magazine › Review article › peer-review

Harvard

Oh, E & Robinson, I 2012, 'Barfly: Sculpting membranes at the Drosophila neuromuscular junction', Developmental Neurobiology, vol. 72, no. 1, pp. 33-56. https://doi.org/10.1002/dneu.20923

APA

Oh, E., & Robinson, I. (2012). Barfly: Sculpting membranes at the Drosophila neuromuscular junction. Developmental Neurobiology, 72(1), 33-56. https://doi.org/10.1002/dneu.20923

Vancouver

Oh E, Robinson I. Barfly: Sculpting membranes at the Drosophila neuromuscular junction. Developmental Neurobiology. 2012 Jan;72(1):33-56. doi: 10.1002/dneu.20923

Author

Oh, Eugene ; Robinson, Iain. / Barfly : Sculpting membranes at the Drosophila neuromuscular junction. In: Developmental Neurobiology. 2012 ; Vol. 72, No. 1. pp. 33-56.

Bibtex

@article{13640d9d4025468397afb0b23f240c46,
title = "Barfly: Sculpting membranes at the Drosophila neuromuscular junction",
abstract = "The ability of a cell to change the shape of its membranes is intrinsic to many cellular functions. Proteins that can alter or recognize curved membrane structures and those that can act to recruit other proteins which stabilize the membrane curvature are likely to be essential in cell functions. The BAR (Bin, amphiphysin, RVS167 homology) domain is a protein domain that can either induce lipidic membranes to curve or can sense curved membranes. BAR domains are found in several proteins at neuronal synapses. We will review BAR domain structure and the role that BAR domain containing proteins play in regulating the morphology and function of the Drosophila neuromuscular junction. In flies the BAR domain containing proteins, endophilin and syndapin affect synaptic vesicle endocytosis, whereas CIP4, dRich, nervous wreck and syndapin affect synaptic morphology. We will review the growing evidence implicating mutations in BAR domain containing proteins being the cause of human pathologies.",
keywords = "BAR domain proteins, Drosophila, Neuromuscular junction",
author = "Eugene Oh and Iain Robinson",
year = "2012",
month = jan,
doi = "10.1002/dneu.20923",
language = "English",
volume = "72",
pages = "33--56",
journal = "Developmental Neurobiology",
issn = "1932-8451",
publisher = "John Wiley and Sons Inc.",
number = "1",

}

RIS

TY - JOUR

T1 - Barfly

T2 - Sculpting membranes at the Drosophila neuromuscular junction

AU - Oh, Eugene

AU - Robinson, Iain

PY - 2012/1

Y1 - 2012/1

N2 - The ability of a cell to change the shape of its membranes is intrinsic to many cellular functions. Proteins that can alter or recognize curved membrane structures and those that can act to recruit other proteins which stabilize the membrane curvature are likely to be essential in cell functions. The BAR (Bin, amphiphysin, RVS167 homology) domain is a protein domain that can either induce lipidic membranes to curve or can sense curved membranes. BAR domains are found in several proteins at neuronal synapses. We will review BAR domain structure and the role that BAR domain containing proteins play in regulating the morphology and function of the Drosophila neuromuscular junction. In flies the BAR domain containing proteins, endophilin and syndapin affect synaptic vesicle endocytosis, whereas CIP4, dRich, nervous wreck and syndapin affect synaptic morphology. We will review the growing evidence implicating mutations in BAR domain containing proteins being the cause of human pathologies.

AB - The ability of a cell to change the shape of its membranes is intrinsic to many cellular functions. Proteins that can alter or recognize curved membrane structures and those that can act to recruit other proteins which stabilize the membrane curvature are likely to be essential in cell functions. The BAR (Bin, amphiphysin, RVS167 homology) domain is a protein domain that can either induce lipidic membranes to curve or can sense curved membranes. BAR domains are found in several proteins at neuronal synapses. We will review BAR domain structure and the role that BAR domain containing proteins play in regulating the morphology and function of the Drosophila neuromuscular junction. In flies the BAR domain containing proteins, endophilin and syndapin affect synaptic vesicle endocytosis, whereas CIP4, dRich, nervous wreck and syndapin affect synaptic morphology. We will review the growing evidence implicating mutations in BAR domain containing proteins being the cause of human pathologies.

KW - BAR domain proteins

KW - Drosophila

KW - Neuromuscular junction

U2 - 10.1002/dneu.20923

DO - 10.1002/dneu.20923

M3 - Review article

C2 - 21630471

AN - SCOPUS:83455217475

VL - 72

SP - 33

EP - 56

JO - Developmental Neurobiology

JF - Developmental Neurobiology

SN - 1932-8451

IS - 1

ER -