Evidence map›Paper›PMID 27718363›Full record

ArticleBiochimica et biophysica acta. Proteins and proteomics2017

Structural pliability adjacent to the kinase domain highlights contribution of FAK1 IDRs to cytoskeletal remodeling.

Jaymin J Kathiriya, Ravi Ramesh Pathak, Alexandr Bezginov, Bin Xue, Vladimir N Uversky, Elisabeth R M Tillier, Vrushank Davé

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochimica et biophysica acta. Proteins and proteomics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 34% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. 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 4 institutions in 3 countries.

Jaymin J KathiriyaMorsani College of Medicine, Department of Pathology and Cell Biology, University of South Florida, Tampa, FL 33612, United States.
Ravi Ramesh PathakMorsani College of Medicine, Department of Pathology and Cell Biology, University of South Florida, Tampa, FL 33612, United States.
Alexandr BezginovDepartment of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada.
Bin XueDepartment of Cell Biology, Microbiology and Molecular Biology, University of South Florida, Tampa, FL 33620, United States.
Vladimir N UverskyDepartment of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, United States; USF Health Byrd Alzheimer's Research Institute, University of South Florida, Tampa, FL 33612, United States; Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russian Federation.
Elisabeth R M TillierDepartment of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada.
Vrushank DavéMorsani College of Medicine, Department of Pathology and Cell Biology, University of South Florida, Tampa, FL 33612, United States; Department of Cancer Biology and Evolution, H. Lee Moffitt Cancer Center and Research Institute, Tampa, FL 33612, United States. Electronic address: vdave@health.usf.edu.
University of South Florida · USUniversity of Toronto · CAMoffitt Cancer Center · USUSF Health Byrd Alzheimer's Institute · US

Funding

Hypoxia Signaling and Spontaneous Pulmonary Fibrosis in a Novel Mouse ModelR21AG047473 · NIA · UNIVERSITY OF SOUTH FLORIDA · PI DAVE, VRUSHANK · 2015 to 2016
$426k
NIA NIH HHS R21 AG047473
6 · The paper itself

Abstract

Therapeutic protein kinase inhibitors are designed on the basis of kinase structures. Here, we define intrinsically disordered regions (IDRs) in structurally hybrid kinases. We reveal that 65% of kinases have an IDR adjacent to their kinase domain (KD). These IDRs are evolutionarily more conserved than IDRs distant to KDs. Strikingly, 36 kinases have adjacent IDRs extending into their KDs, defining a unique structural and functional subset of the kinome. Functional network analysis of this subset of the kinome uncovered FAK1 as topologically the most connected hub kinase. We identify that KD-flanking IDR of FAK1 is more conserved and undergoes more post-translational modifications than other IDRs. It preferentially interacts with proteins regulating scaffolding and kinase activity, which contribute to cytoskeletal remodeling. In summary, spatially and evolutionarily conserved IDRs in kinases may influence their functions, which can be exploited for targeted therapies in diseases including those that involve aberrant cytoskeletal remodeling.

Indexed as

CytoskeletonFocal Adhesion Kinase 1Intrinsically Disordered ProteinsProtein ConformationProtein Processing, Post-TranslationalFocal Adhesion Kinase 1Intrinsically Disordered ProteinsEvolution of kinasesFAK1 signalingHub proteinsIntrinsic disorder in kinasesNetwork medicineProtein-protein interaction networks

Identifiers

PMID27718363
PMCPMC5127739
OpenAlexW2529450131

What OpenQuestion holds

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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.