Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

The Rho-guanine nucleotide exchange factor (RhoGEF) TRIO acts as a key regulator of neuronal migration, axonal outgrowth, axon guidance, and synaptogenesis by activating the GTPase RAC1 and modulating actin cytoskeleton remodeling. Pathogenic variants in TRIO are associated with neurodevelopmental diseases, including intellectual disability (ID) and autism spectrum disorders (ASD). Here, we report the largest international cohort of 24 individuals with confirmed pathogenic missense or nonsense variants in TRIO. The nonsense mutations are spread along the TRIO sequence, and affected individuals show variable neurodevelopmental phenotypes. In contrast, missense variants cluster into two mutational hotspots in the TRIO sequence, one in the seventh spectrin repeat and one in the RAC1-activating GEFD1. Although all individuals in this cohort present with developmental delay and a neuro-behavioral phenotype, individuals with a pathogenic variant in the seventh spectrin repeat have a more severe ID associated with macrocephaly than do most individuals with GEFD1 variants, who display milder ID and microcephaly. Functional studies show that the spectrin and GEFD1 variants cause a TRIO-mediated hyper- or hypo-activation of RAC1, respectively, and we observe a striking correlation between RAC1 activation levels and the head size of the affected individuals. In addition, truncations in TRIO GEFD1 in the vertebrate model X. tropicalis induce defects that are concordant with the human phenotype. This work demonstrates distinct clinical and molecular disorders clustering in the GEFD1 and seventh spectrin repeat domains and highlights the importance of tight control of TRIO-RAC1 signaling in neuronal development.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7058823PMC
http://dx.doi.org/10.1016/j.ajhg.2020.01.018DOI Listing

Publication Analysis

Top Keywords

seventh spectrin
12
spectrin repeat
12
trio associated
8
variants trio
8
trio sequence
8
gefd1 variants
8
trio
7
individuals
6
variants
5
gefd1
5

Similar Publications

Opposite Modulation of RAC1 by Mutations in TRIO Is Associated with Distinct, Domain-Specific Neurodevelopmental Disorders.

Am J Hum Genet

March 2020

Wessex Clinical Genetics, University Hospital Southampton National Health Service Foundation Trust, Southampton SO16 5YA, UK; Human Development and Health, Faculty of Medicine, University of Southampton, Southampton SO16 6YD, UK. Electronic address:

The Rho-guanine nucleotide exchange factor (RhoGEF) TRIO acts as a key regulator of neuronal migration, axonal outgrowth, axon guidance, and synaptogenesis by activating the GTPase RAC1 and modulating actin cytoskeleton remodeling. Pathogenic variants in TRIO are associated with neurodevelopmental diseases, including intellectual disability (ID) and autism spectrum disorders (ASD). Here, we report the largest international cohort of 24 individuals with confirmed pathogenic missense or nonsense variants in TRIO.

View Article and Find Full Text PDF

Previous studies on adult rat and mouse skeletal muscles have shown the spatial association of nitric oxide synthase (NOS) I to the dystrophin complex (DC) in the sarcolemma of type II fibers and, in combination with the NMDA receptor-1 (NMDAR-1), an accumulation of the enzyme at the neuromuscular junctions (NMJ) of this fiber type. Using immunohistochemistry, enzyme histochemistry and alpha-bungarotoxin labeling we report here temporal relationships of NOS I, members of the DC, other components of the cortical cytoskeleton in the junctional and non-junctional sarcolemma as well as of molecules involved in NMJ transmission of either type I or II myofibers especially in head and neck muscles during postnatal rat and mouse development. Fiber typing was performed by specific anti-myosin antibodies.

View Article and Find Full Text PDF

Among 80 hereditary spherocytosis (HS) kindreds studied using denaturing electrophoretic separation of solubilized eythrocyte membrane proteins, we recognized three prominent subsets: HS with isolated spectrin deficiency, HS with combined spectrin and ankyrin deficiency, and HS with band 3 deficiency These three subsets represent more than 80% of the HS kindreds studied. In this study, eight dominant HS kindreds with band 3 deficiency were investigated for band 3 mutations. In three of these kindreds, linkage analyses confirmed the band 3 gene as the culprit gene.

View Article and Find Full Text PDF

The synthesis of mouse erythrocyte membrane proteins by Friend erythroleukemia cells during dimethyl sulfoxide-induced differentiation was studied. Untreated and dimethyl sulfoxide-treated cells were incubated with L-[3H]leucine and the incorporation of radioactivity into total trichloroacetic acid-insoluble proteins and into proteins immunoprecipitated with a multivalent rabbit antibody to mouse erythrocyte membranes was determined. The immunoprecipitated membrane proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and radioactivity was detected by fluorography.

View Article and Find Full Text PDF