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Title: Isoform-specific proteasomal degradation of Rbfox3 during chicken embryonic development

Abstract

Highlights: • Protein stability of Rbfox3 splice isoforms is differentially regulated. • Rbfox3-d31, an Rbfox3 isoform lacking the RRM, is highly susceptible to degradation. • The protein stability of Rbfox3-d31 is regulated by the ubiquitin–proteasome pathway. • Rbfox3-d31 inhibits the nuclear localization of Rbfox2. • Rbfox3-d31 inhibits the splicing activity of Rbfox2. - Abstract: Rbfox3, a neuron-specific RNA-binding protein, plays an important role in neuronal differentiation during development. An isoform Rbfox3-d31, which excludes the 93-nucleotide cassette exon within the RNA recognition motif of chicken Rbfox3, has been previously identified. However, the cellular functions of Rbfox3-d31 remain largely unknown. Here we find that Rbfox3-d31 mRNA is highly expressed during the early developmental stages of the chicken embryo, while Rbfox3-d31 protein is barely detected during the same stage due to its rapid degradation mediated by the ubiquitin–proteasome pathway. Importantly, this degradation is specific to the Rbfox3-d31 isoform and it does not occur with full-length Rbfox3. Furthermore, suppression of Rbfox3-d31 protein degradation with the proteasome inhibitor MG132 attenuates the splicing activity of another Rbfox family member Rbfox2 by altering the subcellular localization of Rbfox2. These results suggest that Rbfox3-d31 functions as a repressor for the splicing activity of the Rbfox family and itsmore » protein level is regulated in an isoform-specific manner in vivo.« less

Authors:
; ;
Publication Date:
OSTI Identifier:
22416705
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 450; Journal Issue: 4; Other Information: Copyright (c) 2014 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CHICKENS; EMBRYOS; IN VIVO; INHIBITION; MESSENGER-RNA; NERVE CELLS; NUCLEOTIDES; ONTOGENESIS; PROTEINS; SPLICING

Citation Formats

Kim, Kee K., Adelstein, Robert S., and Kawamoto, Sachiyo, E-mail: kawamots@mail.nih.gov. Isoform-specific proteasomal degradation of Rbfox3 during chicken embryonic development. United States: N. p., 2014. Web. doi:10.1016/J.BBRC.2014.07.057.
Kim, Kee K., Adelstein, Robert S., & Kawamoto, Sachiyo, E-mail: kawamots@mail.nih.gov. Isoform-specific proteasomal degradation of Rbfox3 during chicken embryonic development. United States. doi:10.1016/J.BBRC.2014.07.057.
Kim, Kee K., Adelstein, Robert S., and Kawamoto, Sachiyo, E-mail: kawamots@mail.nih.gov. Fri . "Isoform-specific proteasomal degradation of Rbfox3 during chicken embryonic development". United States. doi:10.1016/J.BBRC.2014.07.057.
@article{osti_22416705,
title = {Isoform-specific proteasomal degradation of Rbfox3 during chicken embryonic development},
author = {Kim, Kee K. and Adelstein, Robert S. and Kawamoto, Sachiyo, E-mail: kawamots@mail.nih.gov},
abstractNote = {Highlights: • Protein stability of Rbfox3 splice isoforms is differentially regulated. • Rbfox3-d31, an Rbfox3 isoform lacking the RRM, is highly susceptible to degradation. • The protein stability of Rbfox3-d31 is regulated by the ubiquitin–proteasome pathway. • Rbfox3-d31 inhibits the nuclear localization of Rbfox2. • Rbfox3-d31 inhibits the splicing activity of Rbfox2. - Abstract: Rbfox3, a neuron-specific RNA-binding protein, plays an important role in neuronal differentiation during development. An isoform Rbfox3-d31, which excludes the 93-nucleotide cassette exon within the RNA recognition motif of chicken Rbfox3, has been previously identified. However, the cellular functions of Rbfox3-d31 remain largely unknown. Here we find that Rbfox3-d31 mRNA is highly expressed during the early developmental stages of the chicken embryo, while Rbfox3-d31 protein is barely detected during the same stage due to its rapid degradation mediated by the ubiquitin–proteasome pathway. Importantly, this degradation is specific to the Rbfox3-d31 isoform and it does not occur with full-length Rbfox3. Furthermore, suppression of Rbfox3-d31 protein degradation with the proteasome inhibitor MG132 attenuates the splicing activity of another Rbfox family member Rbfox2 by altering the subcellular localization of Rbfox2. These results suggest that Rbfox3-d31 functions as a repressor for the splicing activity of the Rbfox family and its protein level is regulated in an isoform-specific manner in vivo.},
doi = {10.1016/J.BBRC.2014.07.057},
journal = {Biochemical and Biophysical Research Communications},
number = 4,
volume = 450,
place = {United States},
year = {Fri Aug 08 00:00:00 EDT 2014},
month = {Fri Aug 08 00:00:00 EDT 2014}
}