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Nuclear Speckle-Related Protein 70 Binds to Serine/Arginine-Rich Splicing Factor-1 and -2 Via an Arginine/Serine-Like Region and Counteracts Their Alternative Splicing Activity SCIE SCOPUS

Title
Nuclear Speckle-Related Protein 70 Binds to Serine/Arginine-Rich Splicing Factor-1 and -2 Via an Arginine/Serine-Like Region and Counteracts Their Alternative Splicing Activity
Authors
Kim, CHKim, YDChoi, EKKim, HRNa, BRIm, SHJun, CD
Date Issued
2016-03-18
Publisher
American Society for Biochemistry and Molecular Biology Inc.
Abstract
Nuclear speckles are subnuclear storage sites containing pre-mRNA splicing machinery. Proteins assembled in nuclear speckles are known to modulate transcription and pre-mRNA processing. We have previously identified nuclear speckle-related protein 70 (NSrp70) as a novel serine/arginine (SR)-related protein that co-localizes with classical SR proteins such as serine/arginine-rich splicing factor 1 (SRSF1 or ASF/SF2) and SRSF2 (SC35). NSrp70 mediates alternative splice site selection, targeting several pre-mRNAs, including CD44 exon v5. Here we demonstrated that NSrp70 interacts physically with two SR proteins, SRSF1 and SRSF2, and reverses their splicing activity in terms of CD44 exon v5 as exon exclusion. The NSrp70 RS-like region was subdivided into three areas. Deletion of the first arginine/serine-rich-like region (RS1) completely abrogated binding to the SR proteins and to target mRNA and also failed to induce splicing of CD44 exon v5, suggesting that RS1 is critical for NSrp70 functioning. Interestingly, RS1 deletion also resulted in the loss of NSrp70 and SR protein speckle positioning, implying a potential scaffolding role for NSrp70 in nuclear speckles. NSrp70 contains an N-terminal coiled-coil domain that is critical not only for self-oligomerization but also for splicing activity. Consistently, deletion of the coiled-coil domain resulted in indefinite formation of nuclear speckles. Collectively, these results demonstrate that NSrp70 acts as a new molecular counterpart for alternative splicing of target RNA, counteracting SRSF1 and SRSF2 splicing activity.
URI
https://oasis.postech.ac.kr/handle/2014.oak/36470
DOI
10.1074/JBC.M115.689414
ISSN
0021-9258
Article Type
Article
Citation
Journal of Biological Chemistry, vol. 291, no. 12, page. 6169 - 6181, 2016-03-18
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임신혁IM, SIN HYEOG
Dept of Life Sciences
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