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Crystal structure of the Rab binding domain of OCRL1 in complex with Rab8 and functional implications of the OCRL1/Rab8 module for Lowe syndrome

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Crystal structure of the Rab binding domain of OCRL1 in complex with Rab8 and functional implications of the OCRL1/Rab8 module for Lowe syndrome. / Hagemann, Nina; Hou, Xiaomin; Goody, Roger S; Itzen, Aymelt; Erdmann, Kai S.

in: Small GTPases, Jahrgang 3, Nr. 2, 14.07.2012, S. 107-10.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Review › Forschung

Harvard

Hagemann, N, Hou, X, Goody, RS, Itzen, A & Erdmann, KS 2012, 'Crystal structure of the Rab binding domain of OCRL1 in complex with Rab8 and functional implications of the OCRL1/Rab8 module for Lowe syndrome', Small GTPases, Jg. 3, Nr. 2, S. 107-10. https://doi.org/10.4161/sgtp.19380

APA

Hagemann, N., Hou, X., Goody, R. S., Itzen, A., & Erdmann, K. S. (2012). Crystal structure of the Rab binding domain of OCRL1 in complex with Rab8 and functional implications of the OCRL1/Rab8 module for Lowe syndrome. Small GTPases, 3(2), 107-10. https://doi.org/10.4161/sgtp.19380

Vancouver

Hagemann N, Hou X, Goody RS, Itzen A, Erdmann KS. Crystal structure of the Rab binding domain of OCRL1 in complex with Rab8 and functional implications of the OCRL1/Rab8 module for Lowe syndrome. Small GTPases. 2012 Jul 14;3(2):107-10. https://doi.org/10.4161/sgtp.19380

Bibtex

@article{0d1453e7235647aab4683ecc769d517b,
title = "Crystal structure of the Rab binding domain of OCRL1 in complex with Rab8 and functional implications of the OCRL1/Rab8 module for Lowe syndrome",
abstract = "Mutations of the inositol-5-phosphatase OCRL1 cause Lowe syndrome. Lowe syndrome is an inherited disease characterized by renal dysfunction and impaired development of the eye and the nervous system. OCRL1 is a Rab effector protein that can bind to a large number of different Rab proteins. We have recently determined the X-ray structure of the Rab-binding domain of OCRL1 in complex with Rab8. Furthermore, we have characterized point mutations that abolish binding to Rab proteins and cause Lowe syndrome. Here we shortly review our recent biophysical and structural work and discuss possible functional implications of our finding that Rab8 binds with the highest affinity to OCRL1 among the Rab proteins tested. This could direct further work on OCRL1 leading to a better understanding of the complex disease mechanism of Lowe syndrome.",
keywords = "Animals, Crystallography, X-Ray, Humans, Models, Molecular, Oculocerebrorenal Syndrome, Phosphoric Monoester Hydrolases, Point Mutation, Protein Binding, Protein Structure, Tertiary, rab GTP-Binding Proteins, Journal Article, Research Support, Non-U.S. Gov't, Review",
author = "Nina Hagemann and Xiaomin Hou and Goody, {Roger S} and Aymelt Itzen and Erdmann, {Kai S}",
year = "2012",
month = jul,
day = "14",
doi = "10.4161/sgtp.19380",
language = "English",
volume = "3",
pages = "107--10",
journal = "Small GTPases",
issn = "2154-1248",
publisher = "LANDES BIOSCIENCE",
number = "2",

}

RIS

TY - JOUR

T1 - Crystal structure of the Rab binding domain of OCRL1 in complex with Rab8 and functional implications of the OCRL1/Rab8 module for Lowe syndrome

AU - Hagemann, Nina

AU - Hou, Xiaomin

AU - Goody, Roger S

AU - Itzen, Aymelt

AU - Erdmann, Kai S

PY - 2012/7/14

Y1 - 2012/7/14

N2 - Mutations of the inositol-5-phosphatase OCRL1 cause Lowe syndrome. Lowe syndrome is an inherited disease characterized by renal dysfunction and impaired development of the eye and the nervous system. OCRL1 is a Rab effector protein that can bind to a large number of different Rab proteins. We have recently determined the X-ray structure of the Rab-binding domain of OCRL1 in complex with Rab8. Furthermore, we have characterized point mutations that abolish binding to Rab proteins and cause Lowe syndrome. Here we shortly review our recent biophysical and structural work and discuss possible functional implications of our finding that Rab8 binds with the highest affinity to OCRL1 among the Rab proteins tested. This could direct further work on OCRL1 leading to a better understanding of the complex disease mechanism of Lowe syndrome.

AB - Mutations of the inositol-5-phosphatase OCRL1 cause Lowe syndrome. Lowe syndrome is an inherited disease characterized by renal dysfunction and impaired development of the eye and the nervous system. OCRL1 is a Rab effector protein that can bind to a large number of different Rab proteins. We have recently determined the X-ray structure of the Rab-binding domain of OCRL1 in complex with Rab8. Furthermore, we have characterized point mutations that abolish binding to Rab proteins and cause Lowe syndrome. Here we shortly review our recent biophysical and structural work and discuss possible functional implications of our finding that Rab8 binds with the highest affinity to OCRL1 among the Rab proteins tested. This could direct further work on OCRL1 leading to a better understanding of the complex disease mechanism of Lowe syndrome.

KW - Animals

KW - Crystallography, X-Ray

KW - Humans

KW - Models, Molecular

KW - Oculocerebrorenal Syndrome

KW - Phosphoric Monoester Hydrolases

KW - Point Mutation

KW - Protein Binding

KW - Protein Structure, Tertiary

KW - rab GTP-Binding Proteins

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

KW - Review

U2 - 10.4161/sgtp.19380

DO - 10.4161/sgtp.19380

M3 - SCORING: Review article

C2 - 22790198

VL - 3

SP - 107

EP - 110

JO - Small GTPases

JF - Small GTPases

SN - 2154-1248

IS - 2

ER -