Evidence map›Paper›PMID 38432637›Full record

ArticleThe Journal of biological chemistry2024

A neurodevelopmental disorder associated with a loss-of-function missense mutation in RAB35.

Adriana Aguila, Somaya Salah, Gopinath Kulasekaran, Moatasem Shweiki, Nava Shaul-Lotan, Hagar Mor-Shaked, Muhannad Daana, Tamar Harel, Peter S McPherson

Open access · goldAbstract readCase Reports
In one paragraph

Article in The Journal of biological chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 46% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

9 authors at 4 institutions in 2 countries.

Adriana AguilaDepartment of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada.
Somaya SalahDepartment of Genetics, Hadassah Medical Center, Jerusalem, Israel.
Gopinath KulasekaranDepartment of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada.
Moatasem ShweikiNeurosurgery Department, Hadassah Medical Center, Jerusalem, Israel.
Nava Shaul-LotanDepartment of Genetics, Hadassah Medical Center, Jerusalem, Israel.
Hagar Mor-ShakedDepartment of Genetics, Hadassah Medical Center, Jerusalem, Israel; Faculty of Medicine, Hebrew University of Jerusalem, Jerusalem, Israel.
Muhannad DaanaChild Development Centers, Clalit Health Care Services, Yokne'am Illit, Israel.
Tamar HarelDepartment of Genetics, Hadassah Medical Center, Jerusalem, Israel; Faculty of Medicine, Hebrew University of Jerusalem, Jerusalem, Israel.
Peter S McPhersonDepartment of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada. Electronic address: peter.mcpherson@mcgill.ca.
Hadassah Medical Center · ILMontreal Neurological Institute and Hospital · CAHebrew University of Jerusalem · ILClalit Health Services · IL

Funding

CIHR
6 · The paper itself

Abstract

Rab35 (Ras-associated binding protein) is a small GTPase that regulates endosomal membrane trafficking and functions in cell polarity, cytokinesis, and growth factor signaling. Altered Rab35 function contributes to progression of glioblastoma, defects in primary cilia formation, and altered cytokinesis. Here, we report a pediatric patient with global developmental delay, hydrocephalus, a Dandy-Walker malformation, axial hypotonia with peripheral hypertonia, visual problems, and conductive hearing impairment. Exome sequencing identified a homozygous missense variant in the GTPase fold of RAB35 (c.80G>A; p.R27H) as the most likely candidate. Functional analysis of the R27H-Rab35 variant protein revealed enhanced interaction with its guanine-nucleotide exchange factor, DENND1A and decreased interaction with a known effector, MICAL1, indicating that the protein is in an inactive conformation. Cellular expression of the variant drives the activation of Arf6, a small GTPase under negative regulatory control of Rab35. Importantly, variant expression leads to delayed cytokinesis and altered length, number, and Arl13b composition of primary cilia, known factors in neurodevelopmental disease. Our findings provide evidence of altered Rab35 function as a causative factor of a neurodevelopmental disorder.

Indexed as

Mutation, MissenseNeurodevelopmental Disordersrab GTP-Binding ProteinsADP-Ribosylation Factor 6ADP-Ribosylation FactorsCell LineCiliaCytokinesisFemaleGuanine Nucleotide Exchange FactorsHumansLoss of Function MutationMaleModels, MolecularPedigreeProtein Structure, TertiaryADP-Ribosylation Factor 6ADP-Ribosylation FactorsARF6 protein, humanGuanine Nucleotide Exchange FactorsRAB35 protein, humanrab GTP-Binding ProteinscytokinesisGTPaseneurodevelopmental disorderprimary ciliaRab35recessive mutation

Identifiers

PMID38432637
PMCPMC10966776
OpenAlexW4392359840

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.