Evidence map›Paper›PMID 33407999›Full record

ArticleBMB reports2021

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

Seong Heon Kim, Jin-Hwa Cho, Bi-Oh Park, Byoung Chul Park, Jeong-Hoon Kim, Sung Goo Park, Sunhong Kim

Open access · goldAbstract read
In one paragraph

Article in BMB reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 49% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Seong Heon KimDepartment of Functional Genomics, KRIBB School of Biological Science, Korea University of Science and Technology, Daejeon 34113; Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, Korea.
Jin-Hwa ChoDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, Korea.
Bi-Oh ParkDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141; College of Pharmacy, Chungbuk National University, Cheongju 28160, Korea.
Byoung Chul ParkDepartment of Functional Genomics, KRIBB School of Biological Science, Korea University of Science and Technology, Daejeon 34113; Department of Proteome Structural Biology, KRIBB School of Biological Science, Korea University of Science and Technology, Daejeon 34113, Korea.
Jeong-Hoon KimDepartment of Functional Genomics, KRIBB School of Biological Science, Korea University of Science and Technology, Daejeon 34113; Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, Korea.
Sung Goo ParkDepartment of Functional Genomics, KRIBB School of Biological Science, Korea University of Science and Technology, Daejeon 34113; Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, Korea.
Sunhong KimDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141; Department of Biomolecular Science, KRIBB School of Biological Science, Korea University of Science and Technology, Daejeon 34113, Korea.
Korea Research Institute of Bioscience and Biotechnology · KRChungbuk National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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. [BMB Reports 2021; 54(5): 272-277].

Indexed as

Calcium-Binding ProteinsCells, CulturedHumansPhosphorylationReceptors, TransferrinRibosomal Protein S6 Kinases, 90-kDaSerineCalcium-Binding ProteinsReceptors, TransferrinREPS1 protein, humanRibosomal Protein S6 Kinases, 90-kDaSerine

Identifiers

PMID33407999
PMCPMC8167248
OpenAlexW3120222698

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.