Glucosidase, Alpha Neutral AB; Glucosidase II Subunit Beta (GANAB, PRKCSH, α-Glucosidase II)

Nairn, Alison V.; Moremen, Kelley W.

doi:10.1007/978-4-431-54240-7_140

Cited by 3 publications

(3 citation statements)

References 43 publications

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“…Our proteomic results showed a highly significant enrichment of proteins related to the maturation and glycosylation of proteins, including PRKCSH, GANAB, UGGTI, MOGS, CANX, CALR, and ERP29. They all play a role in the calnexin cycle [72]. PRKCSH and GANAB are the regulatory and catalytic subunits of α-glucosidase II, respectively.…”

Section: Discussionmentioning

confidence: 99%

Proteomic Analyses of the G Protein-Coupled Estrogen Receptor GPER1 Reveal Constitutive Links to Endoplasmic Reticulum, Glycosylation, Trafficking, and Calcium Signaling

Ahmadian Elmi,

Motamed,

Picard

2023

Cells

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The G protein-coupled estrogen receptor 1 (GPER1) has been proposed to mediate rapid responses to the steroid hormone estrogen. However, despite a strong interest in its potential role in cancer, whether it is indeed activated by estrogen and how this works remain controversial. To provide new tools to address these questions, we set out to determine the interactome of exogenously expressed GPER1. The combination of two orthogonal methods, namely APEX2-mediated proximity labeling and immunoprecipitation followed by mass spectrometry, gave us high-confidence results for 73 novel potential GPER1 interactors. We found that this GPER1 interactome is not affected by estrogen, a result that mirrors the constitutive activity of GPER1 in a functional assay with a Rac1 sensor. We specifically validated several hits highlighted by a gene ontology analysis. We demonstrate that CLPTM1 interacts with GPER1 and that PRKCSH and GANAB, the regulatory and catalytic subunits of α-glucosidase II, respectively, associate with CLPTM1 and potentially indirectly with GPER1. An imbalance in CLPTM1 levels induces nuclear association of GPER1, as does the overexpression of PRKCSH. Moreover, we show that the Ca2+ sensor STIM1 interacts with GPER1 and that upon STIM1 overexpression and depletion of Ca2+ stores, GPER1 becomes more nuclear. Thus, these new GPER1 interactors establish interesting connections with membrane protein maturation, trafficking, and calcium signaling.

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Section: Discussionmentioning

confidence: 99%

Proteomic Analyses of the G Protein-Coupled Estrogen Receptor GPER1 Reveal Constitutive Links to Endoplasmic Reticulum, Glycosylation, Trafficking, and Calcium Signaling

Ahmadian Elmi,

Motamed,

Picard

2023

Cells

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“…GII activity can be assayed with several substrates. Specifically, natural substrates include Glc 1-2 Man 9 GlcNAc 2 and maltose, but the enzyme does not hydrolyze glucose from Glc 3 Man 9 GlcNAc [370]. The enzyme pH optimum from various organisms ranges from 6 to 7.5 [371][372][373], but the human isoform coming from the human placenta has an even wider pH optimum of 5.5-8.5 [374].…”

Section: Enzyme Activity Assay and Interactions Of Glucosidase IImentioning

confidence: 99%

GANAB and N-Glycans Substrates Are Relevant in Human Physiology, Polycystic Pathology and Multiple Sclerosis: A Review

Masi

Orlando

2022

IJMS

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Glycans are one of the four fundamental macromolecular components of living matter, and they are highly regulated in the cell. Their functions are metabolic, structural and modulatory. In particular, ER resident N-glycans participate with the Glc3Man9GlcNAc2 highly conserved sequence, in protein folding process, where the physiological balance between glycosylation/deglycosylation on the innermost glucose residue takes place, according GANAB/UGGT concentration ratio. However, under abnormal conditions, the cell adapts to the glucose availability by adopting an aerobic or anaerobic regimen of glycolysis, or to external stimuli through internal or external recognition patterns, so it responds to pathogenic noxa with unfolded protein response (UPR). UPR can affect Multiple Sclerosis (MS) and several neurological and metabolic diseases via the BiP stress sensor, resulting in ATF6, PERK and IRE1 activation. Furthermore, the abnormal GANAB expression has been observed in MS, systemic lupus erythematous, male germinal epithelium and predisposed highly replicating cells of the kidney tubules and bile ducts. The latter is the case of Polycystic Liver Disease (PCLD) and Polycystic Kidney Disease (PCKD), where genetically induced GANAB loss affects polycystin-1 (PC1) and polycystin-2 (PC2), resulting in altered protein quality control and cyst formation phenomenon. Our topics resume the role of glycans in cell physiology, highlighting the N-glycans one, as a substrate of GANAB, which is an emerging key molecule in MS and other human pathologies.

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“…[6][7][8][9][10][11] Although, the enzymes exist in monomeric form in prokaryotes, plants and primary eukaryotes, hetero and homodimeric structures were found in advanced Eukaryotes. 1,12 Therefore, the classification of α-Gls enzyme is of great importance for enzymologists and evolutionists. According to Chiba`s classification, Escherichia coli and other bacterial species constitute family I of α-Gls.…”

Section: Introductionmentioning

confidence: 99%

A Computational Comparative Study of Α-Glucosidase Enzyme Divergence

Mehraban¹,

Ghasemi²,

Vallian³

2015

MOJPB

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α-glucosidases (α-Gls) catalyze the last step of carbohydrate digestion in mammals and release glucose in bloodstream, which results in the increased blood glucose level. The evolution and classification of this enzyme has been a matter of debate. In the present study the amino acid sequences of α-Gls from 12 species were aliened and the Phylogenetic trees were constructed. The data indicated that only the mammalian enzyme contained the glucoamylase region. Five amino acid regions were found to be the conservative blocks of mammalian α-Gls. These blocks were not fully conserved in plants, fungi and bacteria. The results were in favor of Chiba`s classification despite the Ile→Thr substitution in Aspergillus Niger and Ala→Pro substitution in chimpanzee and human α-Gls. The chimpanzee α-Gls showed the most similarity to human enzyme. Plants, fungi, bacteria, and the mammalian α-Gls seemed to separately create a specific class. Together, the data suggest that the eukaryotic enzyme had been diverged significantly from the prokaryotic α-Gls since the separation from the common ancestor.

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Glucosidase, Alpha Neutral AB; Glucosidase II Subunit Beta (GANAB, PRKCSH, α-Glucosidase II)

Cited by 3 publications

References 43 publications

Proteomic Analyses of the G Protein-Coupled Estrogen Receptor GPER1 Reveal Constitutive Links to Endoplasmic Reticulum, Glycosylation, Trafficking, and Calcium Signaling

Proteomic Analyses of the G Protein-Coupled Estrogen Receptor GPER1 Reveal Constitutive Links to Endoplasmic Reticulum, Glycosylation, Trafficking, and Calcium Signaling

GANAB and N-Glycans Substrates Are Relevant in Human Physiology, Polycystic Pathology and Multiple Sclerosis: A Review

A Computational Comparative Study of Α-Glucosidase Enzyme Divergence

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