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Tissue-specific alternative RNA splicing of rat vesicle-associated membrane protein-1 (VAMP-1).

Authors: Mandic, R  Trimble, WS  Lowe, AW 
Citation: Mandic R, etal., Gene 1997 Oct 15;199(1-2):173-9.
Pubmed: (View Article at PubMed) PMID:9358054

The vesicle-associated membrane protein (VAMP) family is essential to vesicle-mediated protein transport. Three mammalian isoforms, VAMP-1, VAMP-2, and cellubrevin, play a role in protein transport to the plasma membrane. In this study, we describe a new rat VAMP-1 isoform produced by alternative pre-mRNA splicing. Only one VAMP-1 isoform dominates in each tissue. Analysis of the nucleotide sequence for the newly discovered isoform, VAMP-1b, reveals that its expression is determined by whether an intron is retained or removed. The predicted amino acid sequences for the VAMP-1 isoforms differ at the carboxy-terminal end of the protein. A similar process has been described for VAMPs in Drosophila melanogaster and suggests a conserved function for the carboxy-terminal domain that can be modulated.


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CRRD Object Information
CRRD ID: 1299100
Created: 2004-06-01
Species: All species
Last Modified: 2006-04-25
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.