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Human Molecular Genetics Advance Access originally published online on March 6, 2006
Human Molecular Genetics 2006 15(8):1291-1302; doi:10.1093/hmg/ddl047
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© The Author 2006. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Mpp4 recruits Psd95 and Veli3 towards the photoreceptor synapse

Wendy M. Aartsen1, Albena Kantardzhieva1, Jan Klooster2, Agnes G.S.H. van Rossum1, Serge A. van de Pavert1, Inge Versteeg1, Bob Nunes Cardozo2, Felix Tonagel3, Susanne C. Beck3, Naoyuki Tanimoto3, Mathias W. Seeliger3 and Jan Wijnholds1,*

1Department of Neuromedical Genetics and 2Department of Retinal Signal Processing, The Netherlands Institute for Neuroscience (NIN), Royal Netherlands Academy of Arts and Science (KNAW), Meibergdreef 47, 1105 BA Amsterdam, The Netherlands and 3Retinal Electrodiagnostics Research Group, Department of Ophthalmology, University of Tübingen, Schleichstr. 12-16, 72076 Tübingen, Germany

* To whom correspondence should be addressed at: Department of Neuromedical Genetics, The Netherlands Institute for Neuroscience, Meibergdreef 47, 1105 BA, Amsterdam, The Netherlands. Tel: +31 205664597; Fax: +31 205666121; Email: j.wijnholds{at}nin.knaw.nl

Received November 1, 2005; Revised February 24, 2006; Accepted March 2, 2006

Membrane-associated guanylate kinase (MAGUK) proteins function as scaffold proteins contributing to cell polarity and organizing signal transducers at the neuronal synapse membrane. The MAGUK protein Mpp4 is located in the retinal outer plexiform layer (OPL) at the presynaptic plasma membrane and presynaptic vesicles of photoreceptors. Additionally, it is located at the outer limiting membrane (OLM) where it might be involved in OLM integrity. In Mpp4 knockout mice, loss of Mpp4 function only sporadically causes photoreceptor displacement, without changing the Crumbs (Crb) protein complex at the OLM, adherens junctions or synapse structure. Scanning laser ophthalmology revealed no retinal degeneration. The minor morphological effects suggest that Mpp4 is a candidate gene for mild retinopathies only. At the OPL, Mpp4 is essential for correct localization of Psd95 and Veli3 at the presynaptic photoreceptor membrane. Psd95 labeling is absent of presynaptic membranes in both rods and cones but still present in cone basal contacts and dendritic contacts. Total retinal Psd95 protein levels are significantly reduced which suggests Mpp4 to be involved in Psd95 turnover, whereas Veli3 proteins levels are not changed. These protein changes in the photoreceptor synapse did not result in an altered electroretinograph. These findings suggest that Mpp4 coordinates Psd95/Veli3 assembly and maintenance at synaptic membranes. Mpp4 is a critical recruitment factor to organize scaffolds at the photoreceptor synapse and is likely to be associated with synaptic plasticity and protein complex transport.


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