Phosphorylation of REPS1 at Ser709 by RSK attenuates the recycling of Transferrin receptor

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Title
Phosphorylation of REPS1 at Ser709 by RSK attenuates the recycling of Transferrin receptor
Author(s)
Seong Heon Kim; Jin Hwa Cho; Bi-Oh Park; Byoung Chul ParkJeong Hoon KimSung Goo Park; Sunhong Kim
Bibliographic Citation
BMB Reports, vol. 54, no. 5, pp. 272-277
Publication Year
2021
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.
Keyword
AttenuationPhosphorylationRecyclingRSKTransferrin receptor
ISSN
1976-6696
Publisher
Korea Soc-Assoc-Inst
DOI
http://dx.doi.org/10.5483/bmbrep.2021.54.5.266
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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