Evidence map›Paper›PMID 30158666›Full record

ArticleScientific reports2018

A Serine/Threonine Kinase 16-Based Phospho-Proteomics Screen Identifies WD Repeat Protein-1 As A Regulator Of Constitutive Secretion.

Alfonso López-Coral, Anneliese C Striz, Pamela L Tuma

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

11 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Proteomic Analysis of Pecan (Foods (Basel, Switzerland) · 2023
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Serine/Threonine Protein Kinase STK16.International journal of molecular sciences · 2019
    Review
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

3 authors at 1 institution in 1 country.

Alfonso López-CoralDepartment of Biology, The Catholic University of America, Washington DC, 20064, USA.
Anneliese C StrizDepartment of Biology, The Catholic University of America, Washington DC, 20064, USA.
Pamela L TumaDepartment of Biology, The Catholic University of America, Washington DC, 20064, USA. tuma@cua.edu.
Catholic University of America · US

Funding

MAL2 regulation of hepatic protein trafficking: mechanisms and binding partnersR01DK082890 · NIDDK · CATHOLIC UNIVERSITY OF AMERICA · PI TUMA, PAMELA L. · 2009 to 2012
$774k
NIDDK NIH HHS R01 DK082890U.S. Department of Health & Human Services | NIH | National Institute of Diabetes and Digestive and Kidney Diseases (National Institute of Diabetes & Digestive & Kidney Diseases) DK082890
6 · The paper itself

Abstract

The plasma membrane of polarized hepatocytes is functionally divided into two domains: the apical and basolateral. Our focus is to define the molecular basis of polarized protein sorting of newly-synthesized membrane and secretory proteins in WIF-B cells, an excellent model system for polarized hepatocytes. We determined that MAL2 (myelin and lymphocyte protein 2) and its binding partner, serine/threonine kinase 16 (STK16) regulate basolateral constitutive secretion. Because STK16 is a constitutively active kinase, we reasoned that constitutively phosphorylated substrates must participate in constitutive secretion. To identify either STK16 substrates or other proteins that regulate constitutive secretion, we took a proteomics approach. Post-nuclear supernatants from cells expressing wild type or a kinase-dead (E202A) STK16 were separated on 2D gels and immunoblotted with antibodies against phospho-serine/threonine residues. Sixteen spots were identified from E202A-expressing cells that reproducibly displayed decreased immunoreactivity. From these spots, 28 proteins were identified as possible STK16 substrates. Out of these 28 possible substrates, 25% of them encode predicted STK16 phosphorylation consensus sites, with WD repeat containing protein-1 (WDR1) encoding two such sites. Based on this finding and on the finding that actin remodeling is required for hepatic secretion, we further confirmed that WDR1 is a phosphoprotein that regulates secretion.

Indexed as

Protein TransportAnimalsCell LineElectrophoresis, Gel, Two-DimensionalHepatocytesHumansImmunoblottingMicrofilament ProteinsMyelin and Lymphocyte-Associated Proteolipid ProteinsPhosphoproteinsProtein Serine-Threonine KinasesProteomeRatsTranscription FactorsMAL2 protein, humanMicrofilament ProteinsMyelin and Lymphocyte-Associated Proteolipid ProteinsPhosphoproteinsProtein Serine-Threonine KinasesProteomeSTK16 protein, humanTranscription FactorsWDR1 protein, human

Identifiers

PMID30158666
PMCPMC6115458
OpenAlexW2888532094

What Socratic 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 Socratic graph.