Evidence map›Paper›PMID 38637565›Full record

ArticleScientific reports2024

Xbra modulates the activity of linker region phosphorylated Smad1 during Xenopus development.

Santosh Kumar, Zobia Umair, Vijay Kumar, Ravi Shankar Goutam, Soochul Park, Unjoo Lee, Jaebong Kim

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2024. 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
0.9field-weighted citation impact, top 27% 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, 4 citations in OpenAlex.

  1. Article
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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 3 institutions in 2 countries.

Santosh KumarDepartment of Biochemistry, Institute of Cell Differentiation and Aging, College of Medicine, Hallym University, Chuncheon, Gangwon-Do, 24252, Republic of Korea.
Zobia UmairDepartment of Biochemistry, Institute of Cell Differentiation and Aging, College of Medicine, Hallym University, Chuncheon, Gangwon-Do, 24252, Republic of Korea.
Vijay KumarDepartment of Biochemistry, Institute of Cell Differentiation and Aging, College of Medicine, Hallym University, Chuncheon, Gangwon-Do, 24252, Republic of Korea.
Ravi Shankar GoutamDepartment of Biochemistry, Institute of Cell Differentiation and Aging, College of Medicine, Hallym University, Chuncheon, Gangwon-Do, 24252, Republic of Korea.
Soochul ParkDepartment of Biological Sciences, Sookmyung Women's University, Seoul, 04310, Republic of Korea.
Unjoo LeeDepartment of Electrical Engineering, Hallym University, Chuncheon, Gangwon-Do, 24252, Republic of Korea. ejlee@hallym.ac.kr.
Jaebong KimDepartment of Biochemistry, Institute of Cell Differentiation and Aging, College of Medicine, Hallym University, Chuncheon, Gangwon-Do, 24252, Republic of Korea. jbkim@hallym.ac.kr.
Hallym University · KRSookmyung Women's University · KRUniversité Libre de Bruxelles · BE

Funding

National Research Foundation of Korea 2018M3C7A1056285National Research Foundation of Korea 2021M3H9A1097557National Research Foundation of Korea 2021R1A4A1027355
6 · The paper itself

Abstract

The Bmp/Smad1 pathway plays a crucial role in developmental processes and tissue homeostasis. Mitogen-activated protein kinase (Mapk)/Erk mediated phosphorylation of Smad1 in the linker region leads to Smad1 degradation, cytoplasmic retention and inhibition of Bmp/Smad1 signaling. While Fgf/Erk pathway has been documented to inhibit Bmp/Smad1 signaling, several studies also suggests the cooperative interaction between these two pathways in different context. However, the precise role and molecular pathway of this collaborative interaction remain obscure. Here, we identified Xbra induced by Fgf/Erk signaling as a factor in a protective mechanism for Smad1. Xbra physically interacted with the linker region phosphorylated Smad1 to make Xbra/Smad1/Smad4 trimeric complex, leading to Smad1 nuclear localization and protecting it from ubiquitin-mediated proteasomal degradation. This interaction of Xbra/Smad1/Smad4 led to sustained nuclear localization of Smad1 and the upregulation of lateral mesoderm genes, while concurrently suppression of neural and blood forming genes. Taken together, the results suggests Xbra-dependent cooperative interplays between Fgf/Erk and Bmp/Smad1 signaling during lateral mesoderm specification in Xenopus embryos.

Indexed as

Mitogen-Activated Protein KinasesSignal TransductionAnimalsNervous SystemPhosphorylationSmad1 ProteinXenopus laevisXenopus ProteinsMitogen-Activated Protein KinasesSmad1 ProteinSMAD1 protein, XenopusXenopus ProteinsBmp4ErkFgfMesoderm specificationSmad1Smad4XbraXenopus

Identifiers

PMID38637565
PMCPMC11026473
OpenAlexW4394928586

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.