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Open Access Highly Accessed Research article

Characterization of the transcripts and protein isoforms for cytoplasmic polyadenylation element binding protein-3 (CPEB3) in the mouse retina

Xiang-Ping Wang1 and Nigel GF Cooper12*

Author Affiliations

1 Department of Anatomical Sciences and Neurobiology, Health Sciences Campus, 500 S. Preston Street, University of Louisville, Louisville, KY, USA

2 Department of Ophthalmology and Visual Sciences, Health Sciences Campus, 301 E. Muhammad Ali Boulevard, University of Louisville, Louisville, KY, USA

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BMC Molecular Biology 2009, 10:109  doi:10.1186/1471-2199-10-109

Published: 14 December 2009

Abstract

Background

Cytoplasmic polyadenylation element binding proteins (CPEBs) regulate translation by binding to regulatory motifs of defined mRNA targets. This translational mechanism has been shown to play a critical role in oocyte maturation, early development, and memory formation in the hippocampus. Little is known about the presence or functions of CPEBs in the retina. The purpose of the current study is to investigate the alternative splicing isoforms of a particular CPEB, CPEB3, based on current databases, and to characterize the expression of CPEB3 in the retina.

Results

In this study, we have characterized CPEB3, whose putative role is to regulate the translation of GluR2 mRNA. We identify the presence of multiple alternative splicing isoforms of CPEB3 transcripts and proteins in the current databases. We report the presence of eight alternative splicing patterns of CPEB3, including a novel one, in the mouse retina. All but one of the patterns appear to be ubiquitous in 13 types of tissue examined. The relative abundance of the patterns in the retina is demonstrated. Experimentally, we show that CPEB3 expression is increased in a time-dependent manner during the course of postnatal development, and CPEB3 is localized mostly in the inner retina, including retinal ganglion cells.

Conclusion

The level of CPEB3 was up-regulated in the retina during development. The presence of multiple CPEB3 isoforms indicates remarkable complexity in the regulation and function of CPEB3.