Phosphoproteomics reveals new ERK MAP kinase targets and links ERK to nucleoporin-mediated nuclear transport View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2009-10

AUTHORS

Hidetaka Kosako, Nozomi Yamaguchi, Chizuru Aranami, Masato Ushiyama, Shingo Kose, Naoko Imamoto, Hisaaki Taniguchi, Eisuke Nishida, Seisuke Hattori

ABSTRACT

Many extracellular signal-regulated kinase (ERK) mitogen-activated protein (MAP) kinase substrates have been identified, but the diversity of ERK-mediated processes suggests the existence of additional targets. Using a phosphoproteomic approach combining the steroid receptor fusion system, IMAC, 2D-DIGE and phosphomotif-specific antibodies, we detected 38 proteins showing reproducible phosphorylation changes between ERK-activated and ERK-inhibited samples, including 24 new candidate ERK targets. ERK directly phosphorylated at least 13 proteins in vitro. Of these, Nup50 was verified as a bona fide ERK substrate. Notably, ERK phosphorylation of the FG repeat region of Nup50 reduced its affinity for importin-beta family proteins, importin-beta and transportin. Other FG nucleoporins showed a similar functional change after ERK-mediated phosphorylation. Nuclear migration of importin-beta and transportin was impaired in ERK-activated, digitonin-permeabilized cells, as a result of ERK phosphorylation of Nup50. Thus, we propose that ERK phosphorylates various nucleoporins to regulate nucleocytoplasmic transport. More... »

PAGES

1026-1035

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb.1656

DOI

http://dx.doi.org/10.1038/nsmb.1656

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1019374248

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/19767751


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