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Translation mediated by the nuclear cap-binding complex is confined to the perinuclear region via a CTIF-DDX19B interaction

Authors
Park, YeonkyoungPark, JooriHwang, Hyun JungKim, LeehyeonJeong, KwonSong, Hyun KyuRufener, Simone C.Muehlemann, OliverKim, Yoon Ki
Issue Date
20-8월-2021
Publisher
OXFORD UNIV PRESS
Citation
NUCLEIC ACIDS RESEARCH, v.49, no.14, pp.8261 - 8276
Indexed
SCIE
SCOPUS
Journal Title
NUCLEIC ACIDS RESEARCH
Volume
49
Number
14
Start Page
8261
End Page
8276
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/136830
DOI
10.1093/nar/gkab579
ISSN
0305-1048
Abstract
Newly synthesized mRNA is translated during its export through the nuclear pore complex, when its 5'-cap structure is still bound by the nuclear cap-binding complex (CBC), a heterodimer of cap-binding protein (CBP) 80 and CBP20. Despite its critical role in mRNA surveillance, the mechanism by which CBC-dependent translation (CT) is regulated remains unknown. Here, we demonstrate that the CT initiation factor (CTIF) is tethered in a translationally incompetent manner to the perinuclear region by the DEAD-box helicase 19B (DDX19B). DDX19B hands over CTIF to CBP80, which is associated with the 5'-cap of a newly exported mRNA. The resulting CBP80-CTIF complex then initiates CT in the perinuclear region. We also show that impeding the interaction between CTIF and DDX19B leads to uncontrolled CT throughout the cytosol, consequently dysregulating nonsense-mediated mRNA decay. Altogether, our data provide molecular evidence supporting the importance of tight control of local translation in the perinuclear region.
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