Alternative Splicing Determines the Domain Structure of WWP1, a Nedd4 Family Protein
| Autor: | Patricia Gorman, M. Flasza, Ann E. Canfield, Martin Baron, Rebecca Roylance |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Gene isoform
DNA Complementary Nedd4 Ubiquitin Protein Ligases Ubiquitin-Protein Ligases Molecular Sequence Data Biophysics Exonic splicing enhancer NEDD4 Computational biology Biology Biochemistry Ligases Humans Tissue Distribution splice Amino Acid Sequence RNA Messenger Cloning Molecular Molecular Biology Gene In Situ Hybridization Fluorescence C2 domain Expressed Sequence Tags Genetics Endosomal Sorting Complexes Required for Transport Sequence Homology Amino Acid Reverse Transcriptase Polymerase Chain Reaction Calcium-Binding Proteins Alternative splicing Exons Cell Biology Protein Structure Tertiary Alternative Splicing Multigene Family RNA splicing Chromosomes Human Pair 3 Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 290:431-437 |
| ISSN: | 0006-291X |
| Popis: | Nedd-4-like proteins are E3 ubiquitin-ligase molecules which regulate key trafficking decisions, including targeting of proteins to proteosomes or lysosomes. Here we show that a human Nedd4 family gene, WWP1, is localized on 8q21 and generates at least six isoforms through alternative splicing. We show that alternative splicing affects the domain structure of WWP1, with forms that contain or lack an N-terminal C2 domain. Interestingly, the relative ratio of these forms varies in a tissue-specific manner. Other splice forms were also identified which may disrupt the structure of the C2 domain by removing its predicted C-terminal beta-strands. One splice form generates, through the introduction of a reading frame shift, a C2 domain-only form of WWP1. We discuss the hypothesis that regulation of splice site usage may modulate the activity of WWP1 and possibly other Nedd4 family proteins. |
| Databáze: | OpenAIRE |
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