ERK1/2 interaction with DHPS regulates eIF5A deoxyhypusination independently of ERK kinase activity. Cell Rep 2024 Oct 22;43(10):114831
Date
10/11/2024Pubmed ID
39392755Pubmed Central ID
PMC11544350DOI
10.1016/j.celrep.2024.114831Scopus ID
2-s2.0-85207351264 (requires institutional sign-in at Scopus site) 6 CitationsAbstract
This study explores a non-kinase effect of extracellular regulated kinases 1/2 (ERK1/2) on the interaction between deoxyhypusine synthase (DHPS) and its substrate, eukaryotic translation initiation factor 5A (eIF5A). We report that Raf/MEK/ERK activation decreases the DHPS-ERK1/2 interaction while increasing DHPS-eIF5A association in cells. We determined the cryoelectron microscopy (cryo-EM) structure of the DHPS-ERK2 complex at 3.5 Å to show that ERK2 hinders substrate entrance to the DHPS active site, subsequently inhibiting deoxyhypusination in vitro. In cells, impairing the ERK2 activation loop, but not the catalytic site, prolongs the DHPS-ERK2 interaction irrespective of Raf/MEK signaling. The ERK2 Ser-Pro-Ser motif, but not the common docking or F-site recognition sites, also regulates this complex. These data suggest that ERK1/2 dynamically regulate the DHPS-eIF5A interaction in response to Raf/MEK activity, regardless of its kinase function. In contrast, ERK1/2 kinase activity is necessary to regulate the expression of DHPS and eIF5A. These findings highlight an ERK1/2-mediated dual kinase-dependent and -independent regulation of deoxyhypusination.
Author List
Becker AE, Kochanowski P, Wu PK, Wątor E, Chen W, Guchhait K, Biela AP, Grudnik P, Park JIAuthors
Koushik Guchhait Postdoctoral Researcher 2 in the Biochemistry department at Medical College of WisconsinJong-In Park PhD Professor in the Biochemistry department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
Cryoelectron MicroscopyHEK293 Cells
Humans
MAP Kinase Signaling System
Mitogen-Activated Protein Kinase 1
Mitogen-Activated Protein Kinase 3
Oxidoreductases Acting on CH-NH Group Donors
Peptide Initiation Factors
Protein Binding
RNA-Binding Proteins









