Evidence map›Paper›PMID 27693783›Full record

ArticleBiochemical and biophysical research communications2016

The SH3 domain distinguishes the role of I-BAR proteins IRTKS and MIM in chemotactic response to serum.

Lushen Li, Hongyu Liu, Shaneen S Baxter, Ning Gu, Min Ji, Xi Zhan

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemical and biophysical research communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
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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

6 authors at 4 institutions in 3 countries.

Lushen LiSchool of Biological Science and Medical Engineering, Southeast University, Nanjing 210096, China; The Center for Vascular and Inflammatory Diseases and The Marlene and Stewart Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Hongyu LiuChina-Japan Union Hospital of Jilin University, Changchun, 130031, China.
Shaneen S BaxterThe Center for Vascular and Inflammatory Diseases and The Marlene and Stewart Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Ning GuSchool of Biological Science and Medical Engineering, Southeast University, Nanjing 210096, China.
Min JiSchool of Biological Science and Medical Engineering, Southeast University, Nanjing 210096, China. Electronic address: jimin@seu.edu.cn.
Xi ZhanThe Center for Vascular and Inflammatory Diseases and The Marlene and Stewart Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, MD 21201, USA; Department of Pathology, University of Maryland School of Medicine, Baltimore, MD, USA. Electronic address: xzhan@som.umaryland.edu.
University of Maryland, Baltimore · USSoutheast University · CNSoutheast University · BDUnion Hospital · CN

Funding

Vascular Biology Training ProgramT32HL007698 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI Rosemary A Kozar, Dudley K. Strickland · 1991 to 2026
$8.7M
The Role of MIM in growth factor signaling and cell motilityR01CA113809 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI ZHAN, STEVEN · 2006 to 2016
$2.7M
NCI NIH HHS R01 CA113809NHLBI NIH HHS T32 HL007698
6 · The paper itself

Abstract

The family of inverse BAR (I-BAR) domain proteins participates in a range of cellular processes associated with membrane dynamics and consists of five distinct members. Three of the I-BAR proteins, including insulin receptor tyrosine kinase substrate (IRTKS), contain an SH3 domain near their C-termini. Yet, the function of the SH3 domain of IRTKS remains uncharacterized. Here we report that in contrast to MIM, which is a prototype of I-BAR proteins and does not contain an SH3 domain, IRTKS promoted serum-induced cell migration along with enhanced phosphorylation of mitogen activated kinases Erk1/2 and p38, and activation of small GTPases Rac1 and Cdc42. In addition, cells overexpressing IRTKS exhibited an increased polarity characterized by elongated cytoplasm and extensive lamellipodia at leading edges. However, a mutant with deletion of the SH3 domain attenuated both cellular motility and p38 phosphorylation but had little effect on Erk1/2 phosphorylation. Also, a chimeric mutant in which the N-terminal portion of MIM is fused with the C-terminal IRTKS, including the SH3 domain, was able to promote chemotactic response to serum and cellular polarity. In contrast, a chimeric mutant in which the N-terminal IRTKS is fused with the C-terminal MIM failed to do so. Furthermore, treatment of cells with SB203580, a selective inhibitor of p38, also neutralized the effect of IRTKS on cell migration. These data indicate that the SH3 domain distinguishes the function of IRTKS in promoting cell migration and inducing signal transduction from those of SH3-less I-BAR proteins.

Indexed as

Animalscdc42 GTP-Binding ProteinCell MovementCell ShapeChemotaxisExtracellular Signal-Regulated MAP KinasesHeLa CellsHumansMAP Kinase Signaling SystemMicrofilament ProteinsNeoplasm ProteinsPhosphorylationrac1 GTP-Binding ProteinRecombinant Fusion ProteinsSequence DeletionSignal TransductionBAIAP2L1 protein, humancdc42 GTP-Binding ProteinExtracellular Signal-Regulated MAP KinasesMicrofilament ProteinsMTSS1 protein, humanNeoplasm Proteinsrac1 GTP-Binding ProteinRAC1 protein, humanRecombinant Fusion ProteinsCell migrationCell morphologyIRTKSMIMp38SH3Small GTPases

Identifiers

PMID27693783
PMCPMC5067245
OpenAlexW2525576794

What OpenQuestion holds

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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.