Foerster, Johanna R. and Lochnit, Guenter and Stoehr, Heidi (2009) Proteomic analysis of the membrane palmitoylated protein-4 (MPP4)-associated protein complex in the retina. EXPERIMENTAL EYE RESEARCH, 88 (1). pp. 39-46. ISSN 0014-4835, 1096-0007
Full text not available from this repository. (Request a copy)Abstract
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-beta 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. (C) 2008 Elsevier Ltd. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | IMMUNOCYTOCHEMICAL LOCALIZATION; MAMMALIAN RETINA; SYNAPTIC RIBBONS; MOUSE RETINA; MPP4; KINASE; CELLS; PHOTORECEPTORS; RECOVERIN; PSD-95; MPP4; photoreceptor synapse; protein complex; proteomic approach; Psd95; Hsc70; recoverin |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Humangenetik |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 12 Oct 2020 08:18 |
| Last Modified: | 12 Oct 2020 08:18 |
| URI: | https://pred.uni-regensburg.de/id/eprint/29727 |
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