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http://dx.doi.org/10.5483/BMBRep.2021.54.5.266

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

Kim, Seong Heon (Department of Functional Genomics, KRIBB School of Biological Science, Korea University of Science and Technology)
Cho, Jin-hwa (Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology)
Park, Bi-Oh (Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology)
Park, Byoung Chul (Department of Functional Genomics, KRIBB School of Biological Science, Korea University of Science and Technology)
Kim, Jeong-Hoon (Department of Functional Genomics, KRIBB School of Biological Science, Korea University of Science and Technology)
Park, Sung Goo (Department of Functional Genomics, KRIBB School of Biological Science, Korea University of Science and Technology)
Kim, Sunhong (Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology)
Publication Information
BMB Reports / v.54, no.5, 2021 , pp. 272-277 More about this Journal
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.
Keywords
Attenuation; Phosphorylation; Recycling; RSK; Transferrin receptor;
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