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The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3

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The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3. / Veltel, Stefan; Gasper, Raphael; Eisenacher, Elke; Wittinghofer, Alfred.

In: NAT STRUCT MOL BIOL, Vol. 15, No. 4, 01.04.2008, p. 373-80.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Veltel, S, Gasper, R, Eisenacher, E & Wittinghofer, A 2008, 'The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3', NAT STRUCT MOL BIOL, vol. 15, no. 4, pp. 373-80. https://doi.org/10.1038/nsmb.1396

APA

Veltel, S., Gasper, R., Eisenacher, E., & Wittinghofer, A. (2008). The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3. NAT STRUCT MOL BIOL, 15(4), 373-80. https://doi.org/10.1038/nsmb.1396

Vancouver

Veltel S, Gasper R, Eisenacher E, Wittinghofer A. The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3. NAT STRUCT MOL BIOL. 2008 Apr 1;15(4):373-80. https://doi.org/10.1038/nsmb.1396

Bibtex

@article{efc135b11e4b434a868bed9cfbf9d7e6,
title = "The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3",
abstract = "The retinitis pigmentosa 2 (RP2) gene is responsible for a particular variant of X chromosome-linked eye disease. Previously, RP2 was shown to bind the GTP form of the small G protein Arf-like 3 (Arl3), thus qualifying as an effector. Here we present the Arl3-GppNHp-RP2 complex structure, which shows features resembling complexes with GTPase-activating proteins (GAPs). Biochemical analysis showing a 90,000-fold stimulation of the GTPase reaction together with the structure of an Arl3-GDP-AlF4--RP2 transition state complex showed that RP2 is an efficient GAP for Arl3, with structural features similar to other GAPs. Furthermore, the effect of mutations in patients with retinitis pigmentosa correlated with their effect on catalysis, in particular the mutation of the arginine finger of RP2. The cognate G protein-GAP pair is conserved in yeast as Cin4-Cin2, and the ability of RP2 to act as a GAP can be correlated with its ability to complement a CIN2-deletion phenotype.",
keywords = "ADP-Ribosylation Factors, Animals, Catalysis, Chromatography, Gel, Enzyme Activation, Eye Proteins, GTP Phosphohydrolases, Humans, Intracellular Signaling Peptides and Proteins, Kinetics, Membrane Proteins, Mice",
author = "Stefan Veltel and Raphael Gasper and Elke Eisenacher and Alfred Wittinghofer",
year = "2008",
month = apr,
day = "1",
doi = "10.1038/nsmb.1396",
language = "English",
volume = "15",
pages = "373--80",
journal = "NAT STRUCT MOL BIOL",
issn = "1545-9993",
publisher = "NATURE PUBLISHING GROUP",
number = "4",

}

RIS

TY - JOUR

T1 - The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3

AU - Veltel, Stefan

AU - Gasper, Raphael

AU - Eisenacher, Elke

AU - Wittinghofer, Alfred

PY - 2008/4/1

Y1 - 2008/4/1

N2 - The retinitis pigmentosa 2 (RP2) gene is responsible for a particular variant of X chromosome-linked eye disease. Previously, RP2 was shown to bind the GTP form of the small G protein Arf-like 3 (Arl3), thus qualifying as an effector. Here we present the Arl3-GppNHp-RP2 complex structure, which shows features resembling complexes with GTPase-activating proteins (GAPs). Biochemical analysis showing a 90,000-fold stimulation of the GTPase reaction together with the structure of an Arl3-GDP-AlF4--RP2 transition state complex showed that RP2 is an efficient GAP for Arl3, with structural features similar to other GAPs. Furthermore, the effect of mutations in patients with retinitis pigmentosa correlated with their effect on catalysis, in particular the mutation of the arginine finger of RP2. The cognate G protein-GAP pair is conserved in yeast as Cin4-Cin2, and the ability of RP2 to act as a GAP can be correlated with its ability to complement a CIN2-deletion phenotype.

AB - The retinitis pigmentosa 2 (RP2) gene is responsible for a particular variant of X chromosome-linked eye disease. Previously, RP2 was shown to bind the GTP form of the small G protein Arf-like 3 (Arl3), thus qualifying as an effector. Here we present the Arl3-GppNHp-RP2 complex structure, which shows features resembling complexes with GTPase-activating proteins (GAPs). Biochemical analysis showing a 90,000-fold stimulation of the GTPase reaction together with the structure of an Arl3-GDP-AlF4--RP2 transition state complex showed that RP2 is an efficient GAP for Arl3, with structural features similar to other GAPs. Furthermore, the effect of mutations in patients with retinitis pigmentosa correlated with their effect on catalysis, in particular the mutation of the arginine finger of RP2. The cognate G protein-GAP pair is conserved in yeast as Cin4-Cin2, and the ability of RP2 to act as a GAP can be correlated with its ability to complement a CIN2-deletion phenotype.

KW - ADP-Ribosylation Factors

KW - Animals

KW - Catalysis

KW - Chromatography, Gel

KW - Enzyme Activation

KW - Eye Proteins

KW - GTP Phosphohydrolases

KW - Humans

KW - Intracellular Signaling Peptides and Proteins

KW - Kinetics

KW - Membrane Proteins

KW - Mice

U2 - 10.1038/nsmb.1396

DO - 10.1038/nsmb.1396

M3 - SCORING: Journal article

C2 - 18376416

VL - 15

SP - 373

EP - 380

JO - NAT STRUCT MOL BIOL

JF - NAT STRUCT MOL BIOL

SN - 1545-9993

IS - 4

ER -