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This galley proof is being listed electronically before publishing the final manuscript (It's not final version).

 
Phosphorylation of REPS1 at Ser709 by RSK attenuates the recycling of Transferrin receptor
Sung Goo Park 1,2,*,# (Principal Investigator), Seong Heon Kim1,2 (Researcher), Jin-hwa Cho2 (Researcher), Bi-Oh Park2,3 (Researcher), Byoung Chul Park1,4 (Principal Investigator), Sunhong Kim2,5,6,# (Researcher), Jeonghoon Kim1,2,# (Principal Investigator)
1Functional Genomics, Korea University of Science and Technology,
2Disease Target Structure Research Center, KRIBB,
3College of Pharmacy, Chungbuk National University,
4Proteome Structural Biology and 5Biomolecular Science, Korea University of Science and Technology,
6Drug Discovery Center, LG Chem
Abstract
RalBP1 associated EPS domain containing 1 (REPS1) is conserved from Drosophila to humans and implicated in the endocytic system. However, an exact role of REPS1 remains largely unknown. Here, we demonstrated that mitogen activated protein kinase kinase (MEK)-p90 ribosomal S6 Kinase (RSK) signaling pathway directly phosphorylated REPS1 at Ser709 upon stimulation by epidermal growth factor (EGF) and amino acid. While REPS2 is known to be involved in the endocytosis of EGF receptor (EGFR), REPS1 knockout (KO) cells did not show any defect in the endocytosis of EGFR. However, in the REPS1 KO cells and the KO cells reconstituted with a non-phosphorylatable REPS1 (REPS1 S709A), the recycling of transferrin receptor (TfR) was attenuated compared to the cells reconstituted with wild type REPS1. Collectively, we suggested that the phosphorylation of REPS1 at S709 by RSK may have a role of the trafficking of TfR.
Abstract, Accepted Manuscript(in press) [Submitted on December 2, 2020, Accepted on December 24, 2020]
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