Evidence map›Paper›PMID 32606017›Full record

ArticleMolecular & cellular proteomics : MCP2020

FYN and ABL Regulate the Interaction Networks of the DCBLD Receptor Family.

Anna M Schmoker, Jaye L Weinert, Jacob M Markwood, Kathryn S Albretsen, Michelle L Lunde, Marion E Weir, Alicia M Ebert, Karen L Hinkle, Bryan A Ballif

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed, 1 pooled it
0.4field-weighted citation impact, top 40% 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

4 citing papers in PubMed, 1 synthesis or guideline pooled it, 12 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. 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

9 authors at 2 institutions in 1 country.

Anna M SchmokerDepartment of Biology, University of Vermont, Marsh Life Sciences, Burlington, Vermont, USA. Electronic address: aschmoke@uvm.edu.
Jaye L WeinertDepartment of Biology, University of Vermont, Marsh Life Sciences, Burlington, Vermont, USA.
Jacob M MarkwoodDepartment of Biology, Norwich University, Northfield, Vermont, USA.
Kathryn S AlbretsenDepartment of Biology, Norwich University, Northfield, Vermont, USA.
Michelle L LundeDepartment of Biology, Norwich University, Northfield, Vermont, USA.
Marion E WeirDepartment of Biology, University of Vermont, Marsh Life Sciences, Burlington, Vermont, USA.
Alicia M EbertDepartment of Biology, University of Vermont, Marsh Life Sciences, Burlington, Vermont, USA.
Karen L HinkleDepartment of Biology, Norwich University, Northfield, Vermont, USA.
Bryan A BallifDepartment of Biology, University of Vermont, Marsh Life Sciences, Burlington, Vermont, USA. Electronic address: bballif@uvm.edu.
University of Vermont · USNorwich University Applied Research Institute · US

Funding

Vermont INBRE Administrative Supplement 2024 AWD 118P20GM103449 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI CHRISTOPHER S FRANCKLYN · 2012 to 2026
$58.4M
NIGMS NIH HHS P20 GM103449
6 · The paper itself

Abstract

The Discoidin, CUB, and LCCL domain-containing protein (DCBLD) family consists of two type-I transmembrane scaffolding receptors, DCBLD1 and DCBLD2, which play important roles in development and cancer. The nonreceptor tyrosine kinases FYN and ABL are known to drive phosphorylation of tyrosine residues in YXXP motifs within the intracellular domains of DCBLD family members, which leads to the recruitment of the Src homology 2 (SH2) domain of the adaptors CT10 regulator of kinase (CRK) and CRK-like (CRKL). We previously characterized the FYN- and ABL-driven phosphorylation of DCBLD family YXXP motifs. However, we have identified additional FYN- and ABL-dependent phosphorylation sites on DCBLD1 and DCBLD2. This suggests that beyond CRK and CRKL, additional DCBLD interactors may be regulated by FYN and ABL activity. Here, we report a quantitative proteomics approach in which we map the FYN- and ABL-regulated interactomes of DCBLD family members. We found FYN and ABL regulated the binding of several signaling molecules to DCBLD1 and DCBLD2, including members of the 14-3-3 family of adaptors. Biochemical investigation of the DCBLD2/14-3-3 interaction revealed ABL-induced binding of 14-3-3 family members directly to DCBLD2.

Indexed as

Amino Acid SequenceHEK293 CellsHumansMembrane ProteinsModels, BiologicalPhosphopeptidesPhosphorylationProtein Interaction MapsProto-Oncogene Proteins c-ablProto-Oncogene Proteins c-fynDCBLD1 protein, humanDCBLD2 protein, humanMembrane ProteinsPhosphopeptidesProto-Oncogene Proteins c-ablProto-Oncogene Proteins c-fyn14-3-3ABLDCBLDESDNFYNlabel-free quantificationmass spectrometryPhosphorylationprotein-protein interactionsSILAC

Identifiers

PMID32606017
PMCPMC8015000
OpenAlexW3039157524

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.