Evidence map›Paper›PMID 32321936›Full record

ArticleScientific reports2020

CRISPR-mediated gene targeting of CK1δ/ε leads to enhanced understanding of their role in endocytosis via phosphoregulation of GAPVD1.

Rodrigo X Guillen, Janel R Beckley, Jun-Song Chen, Kathleen L Gould

Abstract read
In one paragraph

Article in Scientific reports, 2020. 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
–field-weighted citation impact
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.

  1. Article
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  5. 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

4 authors.

Rodrigo X GuillenDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.
Janel R BeckleyDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.
Jun-Song ChenDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.
Kathleen L GouldDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA. kathy.gould@vanderbilt.edu.

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI STACIE B DUSETZINA · 1995 to 2026
$172.8M
Translational Analysis CoreP30DK058404 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI RICHARD M. PEEK · 2002 to 2026
$29.9M
Vanderbilt/Meharry Initiative for Minority Student DvptR25GM062459 · NIGMS · VANDERBILT UNIVERSITY · PI VELEZ EDWARDS, DIGNA R · 2002 to 2020
$10.4M
Regulation of cytokinesisR35GM131799 · NIGMS · VANDERBILT UNIVERSITY · PI Kathleen L Gould · 2019 to 2026
$6.4M
Checkpoint control of cytokinesisR01GM112989 · NIGMS · VANDERBILT UNIVERSITY · PI GOULD, KATHLEEN L · 2014 to 2017
$1.5M
NCI NIH HHS P30 CA068485NIDDK NIH HHS P30 DK058404NIGMS NIH HHS R01 GM112989NIGMS NIH HHS R25 GM062459NIGMS NIH HHS R35 GM131799
6 · The paper itself

Abstract

Human casein kinase 1 delta (CK1δ) and epsilon (CK1ε) are members of a conserved family of abundant, ubiquitously expressed serine/threonine kinases that regulate multiple cellular processes including circadian rhythm and endocytosis. Here, we have investigated the localization and interactomes of endogenously tagged CK1δ and CK1ε during interphase and mitosis. CK1δ and CK1ε localize to centrosomes throughout the cell cycle, and in interphase cells to the nucleus, and in both a diffuse and punctate pattern in the cytoplasm. Also, for the first time, they were detected at the midbody during cell division. Mass spectrometry analysis identified a total of 181 proteins co-purifying with a Venus multifunctional (VM)-tagged CK1δ and/or CK1ε. GTPase-activating protein and VPS9 domain-containing protein 1 (GAPVD1), a protein required for efficient endocytosis, was consistently one of the most abundant interacting partners. We demonstrate that GAPVD1 is a substrate of CK1δ/ε with up to 38 phosphorylated residues in vitro and in vivo. Wildtype and a phosphomimetic mutant of GAPVD1, but not a phospho-ablating mutant, were able to rescue defects in transferrin and EGF internalization caused by loss of endogenous GAPVD1. Our results indicate that GAPVD1 is an important interacting partner and substrate of CK1δ/ε for endocytosis.

Indexed as

CRISPR-Cas SystemsCasein Kinase 1 epsilonCasein Kinase IdeltaCell NucleusCentrosomeEndocytosisGene TargetingGuanine Nucleotide Exchange FactorsHEK293 CellsHeLa CellsHumansInterphasePhosphoproteinsPhosphorylationProtein BindingSubstrate SpecificityCasein Kinase 1 epsilonCasein Kinase IdeltaGAPVD1 protein, humanGuanine Nucleotide Exchange FactorsPhosphoproteins

Identifiers

PMID32321936
PMCPMC7176688

What OpenQuestion holds

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Registered trials

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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.