کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
4012159 | 1261181 | 2009 | 10 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Proteomic analysis of the membrane palmitoylated protein-4 (MPP4)-associated protein complex in the retina Proteomic analysis of the membrane palmitoylated protein-4 (MPP4)-associated protein complex in the retina](/preview/png/4012159.png)
Membrane palmitoylated protein-4 (MPP4) is a retina-specific scaffolding protein of the membrane-associated guanylate kinase family that has been implicated in organizing presynaptic protein complexes in the photoreceptor ribbon synapse. To isolate the components of this complex we applied a proteomic approach based on immunoaffinity chromatography with a monoclonal anti-MPP4 antibody followed by two-dimensional electrophoresis and mass spectrometry. Among the identified molecules were previously reported proteins of the MPP4 scaffolding complex including adaptor proteins Veli3 and Psd95. Here we demonstrate a selective association between MPP4 and the Psd95-β isoform that is mediated by interaction of their N-terminal L27 domains. In addition, we have identified recoverin and Hsc70 as novel associated proteins of the MPP4 multiprotein complex in the retina. This study demonstrates the utility of anti-MPP4 antibody precipitation for the elucidation of the MPP4-associated protein complex, which is essential in understanding its precise role in signal transmission at the photoreceptor synapse.
Journal: Experimental Eye Research - Volume 88, Issue 1, 5 January 2009, Pages 39–48