ArticleThe Journal of biological chemistry2014
Identification of a novel protein binding motif within the T-synthase for the molecular chaperone Cosmc.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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.
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.
Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Emerging Roles of the Unique Molecular Chaperone Cosmc in the Regulation of Health and Disease.Biomolecules · 2022Review
- Structural basis for the synthesis of the core 1 structure by C1GalT1.Nature communications · 2022Article
- Review
- C1GALT1 in health and disease.Oncology letters · 2021Review
- A phylogenetic view and functional annotation of the animal β1,3-glycosyltransferases of the GT31 CAZy family.Glycobiology · 2021Article
- Article
- Truncated O-glycans promote epithelial-to-mesenchymal transition and stemness properties of pancreatic cancer cells.Journal of cellular and molecular medicine · 2019Article
- "Stuck on sugars - how carbohydrates regulate cell adhesion, recognition, and signaling".Glycoconjugate journal · 2019Article
- C1GALT1 predicts poor prognosis and is a potential therapeutic target in head and neck cancer.Oncogene · 2018Article
- Article
- [Association of Cosmc gene mutation with susceptibility to Henoch-Schönlein purpura in children].Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2016Article
- Glycosyltransferases and non-alcoholic fatty liver disease.World journal of gastroenterology · 2016Review
- Protein glycosylation in cancer.Annual review of pathology · 2015Review
- Simple sugars to complex disease--mucin-type O-glycans in cancer.Advances in cancer research · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Prior studies suggested that the core 1 β3-galactosyltransferase (T-synthase) is a specific client of the endoplasmic reticulum chaperone Cosmc, whose function is required for T-synthase folding, activity, and consequent synthesis of normal O-glycans in all vertebrate cells. To explore whether the T-synthase encodes a specific recognition motif for Cosmc, we used deletion mutagenesis to identify a cryptic linear and relatively hydrophobic peptide in the N-terminal stem region of the T-synthase that is essential for binding to Cosmc (Cosmc binding region within T-synthase, or CBRT). Using this sequence information, we synthesized a peptide containing CBRT and found that it directly interacts with Cosmc and also inhibits Cosmc-assisted in vitro refolding of denatured T-synthase. Moreover, engineered T-synthase carrying mutations within CBRT exhibited diminished binding to Cosmc that resulted in the formation of inactive T-synthase. To confirm the general recognition of CBRT by Cosmc, we performed a domain swap experiment in which we inserted the stem region of the T-synthase into the human β4GalT1 and found that the CBRT element can confer Cosmc binding onto the β4GalT1 chimera. Thus, CBRT is a unique recognition motif for Cosmc to promote its regulation and formation of active T-synthase and represents the first sequence-specific chaperone recognition system in the ER/Golgi required for normal protein O-glycosylation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.