Document Detail

Crystal structure of the Rab binding domain of OCRL1 in complex with Rab8 and functional implications of the OCRL1/Rab8 module for Lowe syndrome.
MedLine Citation:
PMID:  22790198     Owner:  NLM     Status:  In-Data-Review    
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.
Nina Hagemann; Xiaomin Hou; Roger S Goody; Aymelt Itzen; Kai S Erdmann
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Small GTPases     Volume:  3     ISSN:  2154-1256     ISO Abbreviation:  Small Gtpases     Publication Date:  2012 Apr 
Date Detail:
Created Date:  2012-07-13     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101530974     Medline TA:  Small Gtpases     Country:  United States    
Other Details:
Languages:  eng     Pagination:  107-10     Citation Subset:  IM    
Department of Biochemistry II; Ruhr-University Bochum; Bochum, Germany.
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