ArticleHuman molecular genetics2014
A new congenital disorder of glycosylation caused by a mutation in SSR4, the signal sequence receptor 4 protein of the TRAP complex.
Article in Human molecular genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 69 citations in OpenAlex.
- The TRAP complex (SSR1-SSR4): mechanistic roles and therapeutic opportunities.Annals of medicine · 2026Review
- Clinical and molecular expansion of SSR4-CDG: an adult patient and pathogenic interpretation of an in-frame variant.Journal of human genetics · 2026Article
- SSR4 Sustains Tertiary Lymphoid Structures by Regulation Quality Control of N-linked Glycosylation During B-cell Differentiation Into Plasmacyte in Colorectal Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- The Shape of Things to Come: α-Helical Membrane Protein Folding on the Ribosome.Chemical reviews · 2026Review
- Distinct interleukin-6 production in IPL and TAFRO subtypes of idiopathic multicentric Castleman disease.Haematologica · 2026Article
- Early neonatal diagnosis of SSR4-related congenital disorder of glycosylation with severe congenital heart defects: a case report and systematic review.Frontiers in pediatrics · 2026Article
- Multi-Omics Characterization of a NovelMetabolites · 2025Article
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- Intron retention caused by a canonical splicing variant in SSR4-related congenital disorder of glycosylation.Journal of human genetics · 2025Article
- NovelFrontiers in pediatrics · 2025Article
- Unveiling SSR4: a promising biomarker in esophageal squamous cell carcinoma.Frontiers in immunology · 2025Article
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- A novelFrontiers in genetics · 2024Article
- Molecular view of ER membrane remodeling by the Sec61/TRAP translocon.EMBO reports · 2023Article
- Quantitative Mass Spectrometry Characterizes Client Spectra of Components for Targeting of Membrane Proteins to and Their Insertion into the Membrane of the Human ER.International journal of molecular sciences · 2023Review
- Molecular basis of the TRAP complex function in ER protein biogenesis.Nature structural & molecular biology · 2023Article
- Structural insights into TRAP association with ribosome-Sec61 complex and translocon inhibition by a CADA derivative.Science advances · 2023Article
- Mechanism of Protein Translocation by the Sec61 Translocon Complex.Cold Spring Harbor perspectives in biology · 2023Review
- Case Report: The novel hemizygous mutation in theFrontiers in genetics · 2022Article
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
Nearly 50 congenital disorders of glycosylation (CDG) are known, but many patients biochemically diagnosed with CDG do not have mutations in known genes. Here, we describe a 16-year-old male who was born with microcephaly, developed intellectual disability, gastroesophageal reflux and a seizure disorder. We identified a de novo variant in the X-linked SSR4 gene which encodes a protein of the heterotetrameric translocon-associated protein (TRAP) complex. The c.316delT causes a p.F106Sfs*53 in SSR4 and also reduces expression of other TRAP complex proteins. The glycosylation marker Glyc-ER-GFP was used to confirm the underglycosylation in fibroblasts from the patient. Overexpression of the wild-type SSR4 allele partially restores glycosylation of the marker and of the other members of the TRAP complex. This is the first evidence that the TRAP complex, which binds to the oligosaccharyltransferase complex, is directly involved in N-glycosylation.
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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.