Evidence map›Paper›PMID 25588831›Full record

ArticleJournal of cell science2015

The heterotrimeric kinesin-2 complex interacts with and regulates GLI protein function.

Brandon S Carpenter, Renee L Barry, Kristen J Verhey, Benjamin L Allen

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 48 citations in OpenAlex.

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  13. GLI3: a mediator of genetic diseases, development and cancer.Cell communication and signaling : CCS · 2020
    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 at 1 institution in 1 country.

Brandon S CarpenterDepartment of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Renee L BarryDepartment of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Kristen J VerheyDepartment of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Benjamin L AllenDepartment of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA benallen@umich.edu.
University of Michigan–Ann Arbor · US

Funding

Regional Pilot And Feasibility Study Grants ProgramP30DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Mehboob A Hussain · 2013 to 2026
$24.3M
Regulation of the molecular motor kinesin-IR01GM070862 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI VERHEY, KRISTEN J. · 2005 to 2018
$4.2M
Hedgehog signaling in maintaining taste organ structure and function: basic and clinical studiesR01DC014428 · NIDCD · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ALLEN, BENJAMIN, BRADLEY, ROBERT M · 2015 to 2019
$3.3M
Novel Hedgehog Receptors As Therapeutic Targets In Pancreatic CancerR21CA167122 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ALLEN, BENJAMIN, PASCA DI MAGLIANO, MARINA · 2012 to 2013
$364k
NCI NIH HHS R21 CA167122NIDCD NIH HHS R01 DC014428NIGMS NIH HHS R01 GM070862
6 · The paper itself

Abstract

GLI transport to the primary cilium and nucleus is required for proper Hedgehog (HH) signaling; however, the mechanisms that mediate these trafficking events are poorly understood. Kinesin-2 motor proteins regulate ciliary transport of cargo, yet their role in GLI protein function remains unexplored. To examine a role for the heterotrimeric KIF3A-KIF3B-KAP3 kinesin-2 motor complex in regulating GLI activity, we performed a series of structure-function analyses using biochemical, cell signaling and in vivo approaches that define novel specific interactions between GLI proteins and two components of this complex, KAP3 and KIF3A. We find that all three mammalian GLI proteins interact with KAP3 and we map specific interaction sites in both proteins. Furthermore, we find that GLI proteins interact selectively with KIF3A, but not KIF3B, and that GLI interacts synergistically with KAP3 and KIF3A. Using a combination of cell signaling assays and chicken in ovo electroporation, we demonstrate that KAP3 interactions restrict GLI activator function but not GLI repressor function. These data suggest that GLI interactions with KIF3A-KIF3B-KAP3 complexes are essential for proper GLI transcriptional activity.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsChickensChlorocebus aethiopsCOS CellsCytoskeletal ProteinsHumansKinesinsMicrotubule-Associated ProteinsMultiprotein ComplexesTranscription FactorsTranscription, GeneticZinc Finger Protein GLI1Adaptor Proteins, Signal TransducingCytoskeletal ProteinsGLI1 protein, humanKIF3A protein, humanKIF3B protein, humanKIFAP3 protein, humanKinesinsMicrotubule-Associated ProteinsMultiprotein ComplexesTranscription FactorsZinc Finger Protein GLI1GLIHedgehogKAP3KIF3Kinesin-2

Identifiers

PMID25588831
PMCPMC4342584
OpenAlexW2112771764

What OpenQuestion holds

Textmetadata
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.