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, Vol. 3, No. 2, 14.07.2012, p. 107-10.Research output: SCORING: Contribution to journal › SCORING: Review article › Research
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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 -