MNS5 Antibody

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Description

Introduction to MNS5

MNS5 (AT1G27520 in Arabidopsis thaliana) is a soluble endoplasmic reticulum (ER)-resident enzyme critical for trimming mannose residues on misfolded glycoproteins. It collaborates with MNS4 to regulate ERAD, ensuring protein quality control . Unlike MNS4 (a membrane-associated protein), MNS5 operates in the ER lumen and displays unique substrate preferences .

Table 1: Key Molecular Features of MNS5

PropertyDetail
Gene IDAT1G27520 (Arabidopsis thaliana)
Protein ClassClass I α-1,2-mannosidase (GH47 family)
LocalizationEndoplasmic reticulum lumen
Structure574 amino acids with a signal peptide, lacking transmembrane domain
Enzymatic ActivityTrims terminal α1,2-mannose residues on N-glycans
SubstratesMisfolded glycoproteins (e.g., BRI1 mutants in brassinosteroid signaling)

Role in ERAD and Plant Growth

  • ERAD Regulation: MNS5 demannosylates glycoproteins to generate α1,6-linked mannose residues, marking substrates for ERAD .

  • Suppression of Mutant Phenotypes:

    • The sbi3 mutant (Gly343Glu substitution in MNS5) rescues dwarfism in bri1-5 (BR receptor mutant) by stabilizing misfolded BRI1 variants .

    • MNS5 loss-of-function (mns5-1) reduces ER stress tolerance, impairing growth under tunicamycin or salt stress .

Table 2: Phenotypic Effects of MNS5 Mutants

MutantPhenotypeMechanism
sbi3Suppressed dwarfism in bri1-5, bri1-9, and bri1-235 mutantsStabilizes ERAD substrates via impaired demannosylation
mns5-1Reduced salt and tunicamycin toleranceCompromised ER stress response
mns4-1 mns5-1Enhanced suppression of bri1 mutants compared to single mutantsFunctional redundancy with MNS4

Antibody Development and Applications

While the provided sources do not detail specific commercial MNS5 antibodies, their utility in research includes:

  • Protein Localization: Confirming ER localization via immunofluorescence .

  • Expression Analysis: Detecting MNS5 levels in genetic mutants (e.g., sbi3 shows unchanged mRNA but altered protein activity) .

  • Substrate Interaction Studies: Mapping MNS5’s role in glycoprotein processing using immunoprecipitation .

Research Implications

  • Non-Redundant Function: Unlike MNS4, MNS5 exhibits unique roles in ERAD, as shown by sbi3’s specific suppression of BRI1 mutants without compensatory MNS4 upregulation .

  • Biotechnological Potential: Modulating MNS5 activity could enhance crop stress tolerance by fine-tuning ERAD efficiency .

Future Directions

  • Structural Studies: Resolving MNS5’s 3D architecture to elucidate substrate-binding mechanisms.

  • Antibody Validation: Developing isoform-specific antibodies to distinguish MNS5 from homologous enzymes.

Product Specs

Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
Made-to-order (14-16 weeks)
Synonyms
MNS5 antibody; At1g27520 antibody; T17H3.2 antibody; Alpha-mannosidase I MNS5 antibody; EC 3.2.1.- antibody
Target Names
MNS5
Uniprot No.

Target Background

Function
This antibody can convert Man(9)GlcNAc(2) and Man(8)GlcNAc(2) into N-glycans with a terminal alpha-1,6-linked Man residue in the C-branch. This function is involved in the formation of unique N-glycan structures specifically recognized by components of the endoplasmic reticulum-associated degradation (ERAD) machinery. This recognition leads to the degradation of misfolded glycoproteins. It is likely that this antibody generates an N-glycan signal on misfolded glycoproteins, which is subsequently recognized by OS9. This antibody is essential for the ERAD of the heavily glycosylated and misfolded BRI1 variants BRI1-5 and BRI1-9. It does not appear to play a role in N-glycan processing of correctly folded proteins destined for secretion.
Database Links

KEGG: ath:AT1G27520

STRING: 3702.AT1G27520.1

UniGene: At.24198

Protein Families
Glycosyl hydrolase 47 family
Subcellular Location
Endoplasmic reticulum membrane; Single-pass type II membrane protein.

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