Evidence map›Paper›PMID 37606072›Full record

ArticleThe EMBO journal2023

The IFT81-IFT74 complex acts as an unconventional RabL2 GTPase-activating protein during intraflagellar transport.

Niels Boegholm, Narcis A Petriman, Marta Loureiro-López, Jiaolong Wang, Miren Itxaso Santiago Vela, Beibei Liu, Tomoharu Kanie, Roy Ng, Peter K Jackson, Jens S Andersen and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025
    Review
  3. Review
  4. Article
  5. Review
  6. 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

11 authors at 4 institutions in 2 countries.

Niels Boegholm *Department of Molecular Biology and Genetics, Aarhus University, Aarhus C, Denmark.ORCID 0000-0003-4831-6365
Narcis A Petriman *Department of Molecular Biology and Genetics, Aarhus University, Aarhus C, Denmark.ORCID 0000-0002-3189-7530
Marta Loureiro-LópezDepartment for Biochemistry and Molecular Biology, University of Southern Denmark, Odense M, Denmark.ORCID 0000-0002-6912-6109
Jiaolong WangDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus C, Denmark.
Miren Itxaso Santiago VelaDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus C, Denmark.
Beibei LiuDepartment of Cell Biology, University of Oklahoma Health Science Center, Oklahoma, OK, USA.
Tomoharu KanieDepartment of Cell Biology, University of Oklahoma Health Science Center, Oklahoma, OK, USA.ORCID 0000-0002-2084-1451
Roy NgBaxter Laboratory, Department of Microbiology & Immunology, Stanford University School of Medicine, Stanford, CA, USA.ORCID 0009-0004-4325-4753
Peter K JacksonBaxter Laboratory, Department of Microbiology & Immunology, Stanford University School of Medicine, Stanford, CA, USA.
Jens S AndersenDepartment for Biochemistry and Molecular Biology, University of Southern Denmark, Odense M, Denmark.ORCID 0000-0002-6091-140X
Esben LorentzenDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus C, Denmark.ORCID 0000-0001-6493-7220
Aarhus University · DKStanford University · USUniversity of Oklahoma Health Sciences Center · USUniversity of Southern Denmark · DK

Funding

Tissue Pathology Shared ResourceP30CA225520 · NCI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI ROBERT S. MANNEL · 2018 to 2026
$27.1M
TUMOR RESISTANCE MECHANISMS TO ANTI-VEGF THERAPY IN PROSTATE CANCER (Sukyung Woo)P20GM103639 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI DHANASEKARAN, DANNY N. · 2012 to 2022
$21.3M
NCI NIH HHS P30 CA225520NIGMS NIH HHS P20 GM103639
6 · The paper itself

Abstract

Cilia are important cellular organelles for signaling and motility and are constructed via intraflagellar transport (IFT). RabL2 is a small GTPase that localizes to the basal body of cilia via an interaction with the centriolar protein CEP19 before downstream association with the IFT machinery, which is followed by initiation of IFT. We reconstituted and purified RabL2 with CEP19 or IFT proteins to show that a reconstituted pentameric IFT complex containing IFT81/74 enhances the GTP hydrolysis rate of RabL2. The binding site on IFT81/74 that promotes GTP hydrolysis in RabL2 was mapped to a 70-amino-acid-long coiled-coil region of IFT81/74. We present structural models for RabL2-containing IFT complexes that we validate in vitro and in cellulo and demonstrate that Chlamydomonas IFT81/74 enhances GTP hydrolysis of human RabL2, suggesting an ancient evolutionarily conserved activity. Our results provide an architectural understanding of how RabL2 is incorporated into the IFT complex and a molecular rationale for why RabL2 dissociates from anterograde IFT trains soon after departure from the ciliary base.

Indexed as

GTPase-Activating ProteinsSignal TransductionAmino AcidsBiological TransportCytoskeletal ProteinsGuanosine TriphosphateHumansMuscle ProteinsAmino AcidsCytoskeletal ProteinsGTPase-Activating ProteinsGuanosine TriphosphateIFT74 protein, humanIFT81 protein, humanMuscle ProteinsCiliumGAPGTPaseintraflagellar transportRabL2

Identifiers

PMID37606072
PMCPMC10505919
OpenAlexW4386046868

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.