| First Author | Ohnishi T | Year | 2014 |
| Journal | Genes Cells | Volume | 19 |
| Issue | 2 | Pages | 97-111 |
| PubMed ID | 24251978 | Mgi Jnum | J:215725 |
| Mgi Id | MGI:5606143 | Doi | 10.1111/gtc.12109 |
| Citation | Ohnishi T, et al. (2014) Identification and characterization of a neuron-specific isoform of protrudin. Genes Cells 19(2):97-111 |
| abstractText | Protrudin is a membrane protein that regulates polarized vesicular transport. Now, we have identified a novel isoform of protrudin (protrudin-L) that contains an additional seven amino acids between the FFAT motif and the coiled-coil domain compared with the conventional isoform (protrudin-S) as a result of alternative splicing of a microexon (exon L). Protrudin-L mRNA was found to be mostly restricted to the central nervous system in mice, whereas protrudin-S mRNA was detected in all tissues examined. With the use of a splicing reporter minigene that produces two distinct fluorescent proteins in a manner dependent on the splicing pattern of protrudin transcripts, we found that most neurons express protrudin-L, whereas astrocytes express both protrudin isoforms and oligodendrocytes express only protrudin-S. Protrudin-L associated to a greater extent with vesicle-associated membrane protein-associated protein (VAP) than protrudin-S. Expression of protrudin-L in hippocampal neurons of protrudin-deficient mice also promoted neurite outgrowth more efficiently than protrudin-S. Our results suggest that protrudin-L is a neuron-specific protrudin isoform that promotes axonal elongation and contributes to the establishment of neuronal polarity. |
