Serine 389 phosphorylation of 3-phosphoinositide-dependent kinase 1 by UNC-51-like kinase 1 affects its ability to regulate Akt and p70 S6kinase.

Kidae Kim, Sung Goo Park, Byoung Chul Park, Jeong-Hoon Kim, Sunhong Kim

Open access · goldAbstract read

In one paragraph

Article in BMB reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper, 1 of them a synthesis that pooled it.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed, 1 pooled it

0.2field-weighted citation impact, top 51% 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

1 citing paper in PubMed, 1 synthesis or guideline pooled it, 2 citations in OpenAlex.

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)Autophagy · 2021
Guideline

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

5 authors at 2 institutions in 1 country.

Kidae KimDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141; Department of Proteome Structural biology, KRIBB School of Bioscience, Korea University of Science and Technology, Daejeon 34113, Korea.

Sung Goo ParkDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141; Department of Functional Genomics, KRIBB School of Bioscience, Korea University of Science and Technology, Daejeon 34113, Korea.

Byoung Chul ParkDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141; Department of Proteome Structural biology, KRIBB School of Bioscience, Korea University of Science and Technology, Daejeon 34113, Korea.

Jeong-Hoon KimDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141; Department of Functional Genomics, KRIBB School of Bioscience, Korea University of Science and Technology, Daejeon 34113, Korea.

Sunhong KimDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141; Department of Bio-Molecular Science, KRIBB School of Bioscience, Korea University of Science and Technology, Daejeon 34113, Korea.

Korea Research Institute of Bioscience and Biotechnology · KRKorea University of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphorylation of the signaling component by protein kinase often leads to a kinase cascade or feedback loop. 3-Phosphoinositide- dependent kinase 1 (PDK1) signaling pathway diverges into various kinases including Akt and p70 S6 kinase (p70S6k). However, the PDK1 feedback mechanism remains elusive. Here, we demonstrated that UNC-51-like kinase (ULK1), an autophagy initiator kinase downstream of mechanistic target of rapamycin (mTOR), directly phosphorylated PDK1 on serine 389 at the linker region. Furthermore, our data showed that this phosphorylation affected the kinase activity of PDK1 toward downstream substrates. These results suggest a possible negative feedback loop between PDK1 and ULK1. [BMB Reports 2020; 53(7): 373-378].

Indexed as

3-Phosphoinositide-Dependent Protein KinasesAutophagyAutophagy-Related Protein-1 HomologHEK293 CellsHumansIntracellular Signaling Peptides and ProteinsPhosphatidylinositol 3-KinasePhosphatidylinositolsPhosphorylationProto-Oncogene Proteins c-aktRibosomal Protein S6 Kinases, 70-kDaSerineSignal TransductionTOR Serine-Threonine Kinases3-Phosphoinositide-Dependent Protein KinasesAutophagy-Related Protein-1 HomologIntracellular Signaling Peptides and ProteinsMTOR protein, humanPDPK1 protein, humanPhosphatidylinositol 3-KinasePhosphatidylinositolsProto-Oncogene Proteins c-aktRibosomal Protein S6 Kinases, 70-kDaSerineTOR Serine-Threonine KinasesULK1 protein, human

Identifiers

PMID32317083

PMCPMC7396916

OpenAlexW3017223536

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.