HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Faculty of Pharmaceutical Sciences >
Peer-reviewed Journal Articles, etc >

Structural, super-resolution microscopy analysis of paraspeckle nuclear body organization

Files in This Item:
manuscript.pdf3.42 MBPDFView/Open
supplemental materials.pdfsupplemental materials1.72 MBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/63798

Title: Structural, super-resolution microscopy analysis of paraspeckle nuclear body organization
Authors: West, Jason A. Browse this author
Mito, Mari Browse this author
Kurosaka, Satoshi Browse this author
Takumi, Toru Browse this author →KAKEN DB
Tanegashima, Chiharu Browse this author
Chujo, Takeshi Browse this author
Yanaka, Kaori Browse this author
Kingston, Robert E. Browse this author
Hirose, Tetsuro Browse this author →KAKEN DB
Bond, Charles Browse this author
Fox, Archa Browse this author
Nakagawa, Shinichi Browse this author →KAKEN DB
Issue Date: 27-Sep-2016
Publisher: Rockefeller University Press
Journal Title: Journal of cell biology
Volume: 214
Issue: 7
Start Page: 817
End Page: 830
Publisher DOI: 10.1083/jcb.201601071
Abstract: Paraspeckles are nuclear bodies built on the long noncoding RNA Neat1, which regulates a variety of physiological processes including cancer progression and corpus luteum formation. To obtain further insight into the molecular basis of the function of paraspeckles, we performed fine structural analyses of these nuclear bodies using structural illumination microscopy. Notably, paraspeckle proteins are found within different layers along the radially arranged bundles of Neat1 transcripts, forming a characteristic core-shell spheroidal structure. In cells lacking the RNA binding protein Fus, paraspeckle spheroids are disassembled into smaller particles containing Neat1, which are diffusely distributed in the nucleoplasm. Sequencing analysis of RNAs purified from paraspeckles revealed that AG-rich transcripts associate with Neat1, which are distributed along the shell of the paraspeckle spheroids. We propose that paraspeckles sequester core components inside the spheroids, whereas the outer surface associates with other components in the nucleoplasm to fulfill their function.
Rights: ©West et al., 2016. Originally published in The Journal of Cell Biology. doi:10.1083/jcb.201601071
Type: article
URI: http://hdl.handle.net/2115/63798
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 中川 真一

Export metadata:

OAI-PMH ( junii2 , jpcoar_1.0 )

MathJax is now OFF:


 

 - Hokkaido University