Demonstration of mammalian protein
            <i>O</i>
            -mannosyltransferase activity: Coexpression of POMT1 and POMT2 required for enzymatic activity

Manya, Hiroshi; Chiba, Atsuro; Yoshida, Aruto; Wang, Xiaohui; Chiba, Yasunori; Jigami, Yoshifumi; Margolis, Richard U.; Endo, Tamao

doi:10.1073/pnas.0307228101

Cited by 344 publications

(287 citation statements)

References 44 publications

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“…Second, GnT-III may associate with some other molecules, which define the specificities for protein or peptide substrates. Several studies have shown that the glycosyltransferase complex formation may play a crucial role in the determination of both activity and substrate specificity [35,36]. Third, each glycosyltransferase may have its own pathway to operate glycosylation in Golgi apparatus.…”

Section: Roles Of N-glycosylation On α5β1 Integrinmentioning

confidence: 99%

Potential roles of N-glycosylation in cell adhesion

Isaji

et al. 2012

Glycoconj J

131

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The functional units of cell adhesion are typically multiprotein complexes made up of three general classes of proteins; the adhesion receptors, the cell-extracellular matrix (ECM) proteins, and the cytoplasmic plaque/peripheral membrane proteins. The cell adhesion receptors are usually transmembrane glycoproteins (for example E-cadherin and integrin) that mediate binding at the extracellular surface and determine the specificity of cell-cell and cell-ECM recognition. E-cadherin-mediated cell-cell adhesion can be both temporally and spatially regulated during development, and represents a key step in the acquisition of the invasive phenotype for many tumors. On the other hand, integrin-mediated cell-ECM interactions play important roles in cytoskeleton organization and in the transduction of intracellular signals to regulate various processes such as proliferation, differentiation and cell migration. ECM proteins are typically large glycoproteins, including the collagens, fibronectins, laminins, and proteoglycans that assemble into fibrils or other complex macromolecular arrays. The most of these adhesive proteins are glycosylated. Here, we focus mainly on the modification of N-glycans of integrins and laminin-332, and a mutual regulation between cell adhesion and bisected N-glycan expression, to address the important roles of N-glycans in cell adhesion.

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Section: Roles Of N-glycosylation On α5β1 Integrinmentioning

confidence: 99%

Potential roles of N-glycosylation in cell adhesion

Isaji

et al. 2012

Glycoconj J

131

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“…11, 42 The idea that mutations in both of these genes cause disease is consistent with the demonstration by Endo and colleagues that in flies RNA INTERFERENCE knockdown of POMT1 and POMT2 yields the same phenotype (rotated abdomen), 43 and that coexpression of POMT1 and POMT2 is required for Omannosyltransferase activity in mammalian cell lines. 44 Pomt1 has also been eliminated in mice. 45 The phenotype of these animals-embryonic lethality due to disruption of REICHERT'S MEMBRANE-is the same phenotype that is found in mice lacking Dag1.…”

Section: Dystroglycanopathy-gene Function: Some Mysteries Remainmentioning

confidence: 99%

Mechanisms of Disease: congenital muscular dystrophies—glycosylation takes center stage

Martin

2006

Nat Rev Neurol

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SUMMARYRecent studies have defined a group of muscular dystrophies, now termed the dystroglycanopathies, as novel disorders of glycosylation. These conditions include Walker-Warburg syndrome, muscleeye-brain disease, Fukuyama-type congenital muscular dystrophy, congenital muscular dystrophy types 1C and 1D, and limb-girdle muscular dystrophy type 2I. Although clinical findings can be highly variable, dystroglycanopathies are all characterized by cortical malformations and ocular defects at the more severe end of the clinical spectrum, in addition to muscular dystrophy. All of these disorders are defined by the underglycosylation of α-dystroglycan. Defective glycosylation of dystroglycan severs the link between this important cell adhesion molecule and the extracellular matrix, thereby contributing to cellular pathology. Recent experiments indicate that glycosylation might not only define forms of muscular dystrophy but also provide an avenue to the development of therapies for these disorders.

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“…3 Protein O-mannosyltransferase 2 (POMT2) is a 21-exon gene that encodes an integral membrane protein of the endoplasmic reticulum required for the correct glycosylation of a-dystroglycan. 4,5 Both POMT1 and POMT2 mutations are the most common causes of WWS. 1, 2,6,7 Cardiac involvement among the dystroglycanopathies remains poorly characterized.…”

Section: Introductionmentioning

confidence: 99%

Novel cardiovascular findings in association with a POMT2 mutation: three siblings with α-dystroglycanopathy

Martinez¹,

Craigen

Ummat

et al. 2013

Eur J Hum Genet

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Dystroglycanopathies are a genetically heterogeneous subset of congenital muscular dystrophies that exhibit autosomal recessive inheritance and are characterized by abnormal glycosylation of a-dystroglycan. In particular, POMT2 (protein O-mannosyltransferase-2) mutations have been identified in congenital muscular dystrophy patients with a wide range of clinical involvement, ranging from the severe muscle-eye-brain disease and Walker-Warburg syndrome to limb girdle muscular dystrophy without structural brain or ocular involvement. Cardiovascular disease is thought to be uncommon in congenital muscular dystrophy, with rare reports of cardiac involvement. We describe three brothers aged 21, 19, and 17 years with an apparently homozygous POMT2 mutation who all presented with congenital muscular dystrophy, intellectual disabilities, and distinct cardiac abnormalities. All three brothers were homozygous for a p.Tyr666Cys missense mutation in exon 19 of the POMT2 gene. On screening echocardiograms, all siblings demonstrated significant dilatation of the aortic root and depressed left ventricular systolic function and/or left ventricular wall motion abnormalities. Our report is the first to document an association between POMT2 mutations and aortopathy with concomitant depressed left ventricular systolic function. On the basis of our findings, we suggest patients with POMT2 gene mutations be screened not only for myocardial dysfunction but also for aortopathy. In addition, given the potential for progression of myocardial dysfunction and/or aortic dilatation, longitudinal surveillance imaging is recommended both for patients with disease as well as those that have normal baseline imaging.

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Demonstration of mammalian protein O -mannosyltransferase activity: Coexpression of POMT1 and POMT2 required for enzymatic activity

Cited by 344 publications

References 44 publications

Potential roles of N-glycosylation in cell adhesion

Potential roles of N-glycosylation in cell adhesion

Mechanisms of Disease: congenital muscular dystrophies—glycosylation takes center stage

Novel cardiovascular findings in association with a POMT2 mutation: three siblings with α-dystroglycanopathy

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