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MBC in Press, published online ahead of print May 25, 2005
Mol. Biol. Cell 10.1091/mbc.E05-02-0120

A more recent version of this article appeared on August 1, 2005
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Submitted on February 11, 2005
Revised on May 9, 2005
Accepted on May 12, 2005

Lowe Syndrome Protein OCRL1 Interacts with Clathrin and Regulates Protein Trafficking between Endosomes and the Trans-Golgi Network

Rawshan Choudhury,* Aipo Diao,* Fang Zhang,{dagger} Evan Eisenberg,{dagger} Agnes Saint-Pol,{ddagger} Catrin Williams,* Athanasios Konstantakopoulos,{sect} John Lucocq,{sect} Ludger Johannes,{ddagger} Catherine Rabouille,|| Lois E. Greene,{dagger} and Martin Lowe*

*Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom; {dagger}Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892; {ddagger}Traffic and Signaling Laboratory, Department of Cellular Compartmentalization and Dynamics, UMR 144 Curie/CNRS, Curie Institute, F-75248 Paris Cedex 05, France; ||UMC Utrecht, Department of Cell Biology, AZU, 3584 CX Utrecht, The Netherlands; {sect}School of Life Sciences, University of Dundee, Dundee DD1 5EH, United Kingdom

Monitoring Editor: Sean Munro

Oculocerebrorenal syndrome of Lowe is caused by mutation of OCRL1, a phosphatidylinositol 4,5-bisphosphate 5-phosphatase localized at the Golgi apparatus. The cellular role of OCRL1 is unknown, and consequently the mechanism by which loss of OCRL1 function leads to disease is ill defined. Here, we show that OCRL1 is associated with clathrin-coated transport intermediates operating between the TGN and endosomes. OCRL1 interacts directly with clathrin heavy chain and promotes clathrin assembly in vitro. Interaction with clathrin is not, however, required for membrane association of OCRL1. Overexpression of OCRL1 results in redistribution of clathrin and the cation-independent mannose 6-phosphate receptor (CI-MPR) to enlarged endosomal structures that are defective in retrograde trafficking to the TGN. Depletion of cellular OCRL1 also causes a partial redistribution of a CI-MPR reporter to early endosomes. These findings suggest a role for OCRL1 in clathrin-mediated trafficking of proteins from endosomes to the TGN, and that defects in this pathway might contribute to the Lowe syndrome phenotype.

Address correspondence to: Martin Lowe (lowe{at}man.ac.uk)




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