Modulation of an RNA-binding protein by abscisic-acid-activated protein kinase

Jiaxu Li (), Toshinori Kinoshita, Sona Pandey, Carl K.-Y. Ng, Steven P. Gygi, Ken-ichiro Shimazaki and Sarah M. Assmann ()
Additional contact information
Jiaxu Li: The Pennsylvania State University, 208 Mueller Laboratory
Toshinori Kinoshita: Kyushu University
Sona Pandey: The Pennsylvania State University, 208 Mueller Laboratory
Carl K.-Y. Ng: The Pennsylvania State University, 208 Mueller Laboratory
Steven P. Gygi: Harvard Medical School
Ken-ichiro Shimazaki: Kyushu University
Sarah M. Assmann: The Pennsylvania State University, 208 Mueller Laboratory

Nature, 2002, vol. 418, issue 6899, 793-797

Abstract: Abstract Protein kinases are involved in stress signalling in both plant and animal systems. The hormone abscisic acid mediates the responses of plants to stresses such as drought, salinity and cold. Abscisic-acid-activated protein kinase (AAPK)—found in guard cells, which control stomatal pores—has been shown to regulate plasma membrane ion channels1. Here we show that AAPK-interacting protein 1 (AKIP1), with sequence homology to heterogeneous nuclear RNA-binding protein A/B, is a substrate of AAPK. AAPK-dependent phosphorylation is required for the interaction of AKIP1 with messenger RNA that encodes dehydrin, a protein implicated in cell protection under stress conditions. AAPK and AKIP1 are present in the guard-cell nucleus, and in vivo treatment of such cells with abscisic acid enhances the partitioning of AKIP1 into subnuclear foci which are reminiscent of nuclear speckles. These results show that phosphorylation-regulated RNA target discrimination by heterogeneous nuclear RNA-binding proteins2 may be a general phenomenon in eukaryotes, and implicate a plant hormone in the regulation of protein dynamics during rapid subnuclear reorganization.

Date: 2002
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature00936 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:418:y:2002:i:6899:d:10.1038_nature00936

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature00936

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().