%0 Journal Article
%T Identification and expression analysis of splice variants of mouse enabled homologue during development and in adult tissues
%A Sylvie Veniere
%A Davy Waterschoot
%A Jo£żl Vandekerckhove
%A Anja Lambrechts
%A Christophe Ampe
%J BMC Molecular Biology
%D 2010
%I BioMed Central
%R 10.1186/1471-2199-11-45
%X In silico analysis of the vertebrate Ena/VASP gene family reveals that birds do not have Vasp, while fish have two Evl genes. Analysis of expressed sequence tags of vertebrate Enah splice variants confirms that an Enah transcript without alternative exons is ubiquitously expressed, but yields only limited information about the existence of other possible alternatively spliced Enah transcripts. Via a RT-PCR screen, we provide evidence that during mouse development and in adult mice at least eight and maximally sixteen different Enah transcripts are expressed. We also show that tissues and cell lines display specific expression profiles of these different transcripts. Exons previously associated with neuronal expression of Enah splice variants are also present in other tissues, in particular in heart.We propose a more uniform nomenclature for alternative exons in Enah. We provide an overview of distinct expression profiles of mouse Enah splice variants during mouse development, in adult mouse tissues and in a subset of mouse cell lines.The vertebrate Enabled/Vasodilator stimulated phosphoprotein (Ena/VASP) gene family encodes three proteins: enabled homologue (ENAH, throughout the manuscript we use protein, gene and mRNA symbols based on the format of mouse and rat nomenclature, i.e. ENAH, Enah and Enah, respectively) (also referred to as mammalian enabled or Mena), VASP and Ena-VASP like (EVL). Ena/VASP proteins are actin binding proteins that are involved in dynamic actin remodeling important for maintaining cell shape and cell movement (for review see [1]). These proteins are composed of four conserved domains. An N-terminal Ena/VASP homology domain 1 (EVH1) interacts with different proteins and is especially important for localization of ENA/VASP proteins in the cell. The central proline-rich region binds to the actin binding protein profilin and Src homology 3 (SH3) and WW domains. The EVH2 domain comprises the globular actin (G-actin) and filamentous actin (F-ac
%U http://www.biomedcentral.com/1471-2199/11/45