A novel role for the nuclear localization signal in regulating hnRNP K protein stability in vivo
Abstract
hnRNP K is a highly conserved nucleocytoplasmic shuttling protein, which associates with RNAs through synergistic binding via its three KH domains. hnRNP K is required for proper nuclear export and translational control of its mRNA targets, and these processes are controlled by hnRNP K's movement between subcellular compartments. Whereas the nuclear export and localization of hnRNP K that is associated with mRNP complexes has been well studied, the trafficking of hnRNP K that is unbound to mRNA has yet to be elucidated. To that end, we expressed an EGFP-tagged RNA binding-defective form of hnRNP K in intact Xenopus embryos, and found it was rapidly degraded in vivo. Deleting hnRNP K's nuclear localization signal (NLS), which contains two prospective ubiquitination sites, rescued the protein from degradation. These data demonstrate a novel activity for the NLS of hnRNP K in regulating the protein's stability in vivo when it is unbound to nucleic acids.
Additional Information
© 2016 Elsevier Inc. Received 18 July 2016; Accepted 4 August 2016; Available online 5 August 2016. A National Science Foundation grant (IOS 1257449; BGS), and an American Association of University Women Fellowship (EJH) and Sigma Xi Grant-in-Aid (EJH) supported the work. We thank Dr. Christine Gervasi for providing Xenopus spawnings, Dr. Chen Wang for helpful editorial comments, and Stefanos Haddad for aiding mutagenesis experiments. All the authors declare that there is no conflict of interest in this paper.Additional details
- Eprint ID
- 71201
- Resolver ID
- CaltechAUTHORS:20161018-080013295
- IOS 1257449
- NSF
- American Association of University Women
- Sigma Xi
- Created
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2016-10-18Created from EPrint's datestamp field
- Updated
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2021-11-11Created from EPrint's last_modified field