Literature DB >> 33507475

Clinical, radiological and computational studies on two novel GNPTG variants causing mucolipidosis III gamma phenotypes with varying severity.

Mustafa Doğan1, Recep Eröz2, Kerem Terali3,4, Alper Gezdirici5, Semih Bolu6.   

Abstract

Mucolipidosis III gamma (ML III γ) is a slowly progressive disorder that affects multiple parts of the body such as the skeleton, joints, and connective tissue structures. It is caused by pathogenic variants in the GNPTG gene that provides instructions for producing the γ subunit of GlcNAc-1-phosphotransferase. In this study we aim to characterize clinical findings and biological insights on two novel GNPTG variants causing ML III γ phenotypes with varying severity. We report on two siblings with ML III γ bearing the previously undescribed c.477C > G (p.Y159*) nonsense variant in a homozygous state as well as a patient with ML III γ bearing the novel c.110 + 19_111-17del variant in a homozygous state. These variants were revealed by whole-exome sequencing and Sanger sequencing, respectively. Their parents, who are heterozygotes for the same mutation, are healthy. The clinical and radiographic presentation of ML III γ in our patients who had c.477C > G (p.Y159*) variant is consistent with a relatively severe form of the disease, which is further supported by a working three-dimensional model of the GlcNAc-1-phosphotransferase γ subunit. On the other hand, it is seen that our patient who carries the c.110 + 19_111-17del variant has a milder phenotype. Our findings help broaden the spectrum of GNPTG variants causing ML III γ and offer structural and mechanistic insights into loss of GlcNAc-1-phosphotransferase γ subunit function.

Entities:  

Keywords:  GNPTG; GlcNAc-1-phosphotransferase; Lysosomal storage disorder; Mucolipidosis III gamma

Mesh:

Substances:

Year:  2021        PMID: 33507475     DOI: 10.1007/s11033-021-06158-7

Source DB:  PubMed          Journal:  Mol Biol Rep        ISSN: 0301-4851            Impact factor:   2.316


  31 in total

1.  Mucolipidosis II is caused by mutations in GNPTA encoding the alpha/beta GlcNAc-1-phosphotransferase.

Authors:  Stephan Tiede; Stephan Storch; Torben Lübke; Bernard Henrissat; Ruth Bargal; Annick Raas-Rothschild; Thomas Braulke
Journal:  Nat Med       Date:  2005-10-02       Impact factor: 53.440

2.  Template-based protein structure modeling using the RaptorX web server.

Authors:  Morten Källberg; Haipeng Wang; Sheng Wang; Jian Peng; Zhiyong Wang; Hui Lu; Jinbo Xu
Journal:  Nat Protoc       Date:  2012-07-19       Impact factor: 13.491

3.  Structural requirements for efficient processing and activation of recombinant human UDP-N-acetylglucosamine:lysosomal-enzyme-N-acetylglucosamine-1-phosphotransferase.

Authors:  Mariko Kudo; William M Canfield
Journal:  J Biol Chem       Date:  2006-02-28       Impact factor: 5.157

4.  Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation.

Authors:  Tadashi Satoh; Yang Chen; Dan Hu; Shinya Hanashima; Kazuo Yamamoto; Yoshiki Yamaguchi
Journal:  Mol Cell       Date:  2010-12-22       Impact factor: 17.970

5.  A key enzyme in the biogenesis of lysosomes is a protease that regulates cholesterol metabolism.

Authors:  Katrin Marschner; Katrin Kollmann; Michaela Schweizer; Thomas Braulke; Sandra Pohl
Journal:  Science       Date:  2011-07-01       Impact factor: 47.728

6.  Molecular basis of variant pseudo-hurler polydystrophy (mucolipidosis IIIC)

Authors:  A Raas-Rothschild; V Cormier-Daire; M Bao; E Genin; R Salomon; K Brewer; M Zeigler; H Mandel; S Toth; B Roe; A Munnich; W M Canfield
Journal:  J Clin Invest       Date:  2000-03       Impact factor: 14.808

7.  A novel mutation in UDP-N-acetylglucosamine-1-phosphotransferase gamma subunit (GNPTAG) in two siblings with mucolipidosis type III alters a used glycosylation site.

Authors:  Stephan Tiede; Michael Cantz; Annick Raas-Rothschild; Nicole Muschol; Friederike Bürger; Kurt Ullrich; Thomas Braulke
Journal:  Hum Mutat       Date:  2004-12       Impact factor: 4.878

8.  Bovine UDP-N-acetylglucosamine:lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase. II. Enzymatic characterization and identification of the catalytic subunit.

Authors:  M Bao; B J Elmendorf; J L Booth; R R Drake; W M Canfield
Journal:  J Biol Chem       Date:  1996-12-06       Impact factor: 5.157

9.  Bovine UDP-N-acetylglucosamine:lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase. I. Purification and subunit structure.

Authors:  M Bao; J L Booth; B J Elmendorf; W M Canfield
Journal:  J Biol Chem       Date:  1996-12-06       Impact factor: 5.157

Review 10.  Mannose phosphorylation in health and disease.

Authors:  Katrin Kollmann; Sandra Pohl; Katrin Marschner; Marisa Encarnação; Imme Sakwa; Stephan Tiede; Ben J Poorthuis; Torben Lübke; Sven Müller-Loennies; Stephan Storch; Thomas Braulke
Journal:  Eur J Cell Biol       Date:  2009-11-28       Impact factor: 4.492

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