Specific interaction with the nuclear transporter importin α2 can modulate paraspeckle protein 1 delivery to nuclear paraspeckles

Major, Andrew T., Hogarth, Cathryn A., Miyamoto, Yoichi, Sarraj, Mai A., Smith, Catherine L., Koopman, Peter, Kurihara, Yasuyuki, Jans, David A. and Loveland, Kate L. (2015) Specific interaction with the nuclear transporter importin α2 can modulate paraspeckle protein 1 delivery to nuclear paraspeckles. Molecular Biology of the Cell, 26 8: 1543-1558. doi:10.1091/mbc.E14-01-0678

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Author Major, Andrew T.
Hogarth, Cathryn A.
Miyamoto, Yoichi
Sarraj, Mai A.
Smith, Catherine L.
Koopman, Peter
Kurihara, Yasuyuki
Jans, David A.
Loveland, Kate L.
Title Specific interaction with the nuclear transporter importin α2 can modulate paraspeckle protein 1 delivery to nuclear paraspeckles
Journal name Molecular Biology of the Cell   Check publisher's open access policy
ISSN 1939-4586
Publication date 2015-04-15
Year available 2015
Sub-type Article (original research)
DOI 10.1091/mbc.E14-01-0678
Open Access Status File (Publisher version)
Volume 26
Issue 8
Start page 1543
End page 1558
Total pages 16
Place of publication Bethesda, MD United States
Publisher American Society for Cell Biology
Collection year 2016
Language eng
Abstract Importin (IMP) superfamily members mediate regulated nucleocytoplasmic transport, which is central to key cellular processes. Although individual IMPα proteins exhibit dynamic synthesis and subcellular localization during cellular differentiation, including during spermatogenesis, little is known of how this affects cell fate. To investigate how IMPαs control cellular development, we conducted a yeast two-hybrid screen for IMPα2 cargoes in embryonic day 12.5 mouse testis, a site of peak IMPα2 expression coincident with germ-line masculization. We identified paraspeckle protein 1 (PSPC1), the original defining component of nuclear paraspeckles, as an IMPα2-binding partner. PSPC1-IMPα2 binding in testis was confirmed in immunoprecipitations and pull downs, and an enzyme-linked immunosorbent assay–based assay demonstrated direct, high-affinity PSPC1 binding to either IMPα2/IMPβ1 or IMPα6/IMPβ1. Coexpression of full-length PSPC1 and IMPα2 in HeLa cells yielded increased PSPC1 localization in nuclear paraspeckles. High-throughput image analysis of >3500 cells indicated IMPα2 levels can directly determine PSPC1-positive nuclear speckle numbers and size; a transport-deficient IMPα2 isoform or small interfering RNA knockdown of IMPα2 each reduced endogenous PSPC1 accumulation in speckles. This first validation of an IMPα2 nuclear import cargo in fetal testis provides novel evidence that PSPC1 delivery to paraspeckles, and consequently paraspeckle function, may be controlled by modulated synthesis of specific IMPs.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
Institute for Molecular Bioscience - Publications
 
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