SMG5 Antibodies

Background

SMG5 encodes a key protein involved in the nonsense mediated mRNA degradation (NMD) pathway, which is an important mRNA quality control mechanism in eukaryotic cells. As a core component of the NMD complex, the SMG5 protein regulates the phosphorylation status of the UPF1 protein by forming a heterodimer with SMG7 and recruiting the dephosphorylase PP2A, thereby determining the degradation fate of the targeted mRNA. Research has found that SMG5 plays a significant role in physiological processes such as embryonic development, neural function, and immune regulation, and its abnormal function is associated with the occurrence of various genetic diseases and cancers. This gene was first identified in the RNAi screening experiment for Caenorhabditis elegans in 2003. Its conserved 14-3-3-like domain and prion-like domain provide an ideal model for studying protein-protein interactions. The continuous research on SMG5 not only deepens the understanding of the NMD mechanism but also provides new ideas for the development of treatment strategies for related diseases.

Structure Function Application Advantage Our Products

Structure of SMG5

SMG5 is a protein with a molecular weight of approximately 80-90 kDa, and its precise molecular weight varies slightly due to species and post-translational modifications.

Species	Human	Mouse	Fruit fly	Nematode
Molecular Weight (kDa)	85	83	78	82
Primary Structural Differences	With the 14-3-3 sample structure domain and structure domain of prions samples	Highly conservative and functionally similar	Simplify the NMD mechanism	Early research model

The SMG5 protein is composed of multiple functional domains. Its core includes a conserved 14-3-3-like domain responsible for mediating protein-protein interactions, as well as a prion-like domain that may be involved in phase separation and complex assembly. This protein plays a key role in the nonsense mediated mRNA degradation (NMD) pathway. By forming a heterodimer with SMG7, it regulates the dephosphorylation of UPF1, thereby influencing the stability of targeted mRNA. The secondary structure of SMG5 is mainly composed of α-helix and β-folding, and its conformational changes directly affect the activity of the NMD complex.

Fig. 1:Representation of the SMG5 domain structure. Fig. 1 Schematic representation of the SMG5 domain structure.¹

Key structural properties of SMG5:

14-3-3 sample domains
Prion-like domains
Conserved phosphorylation sites
Disordered area at the C-end

Functions of SMG5

The core function of the SMG5 gene is to participate in the nonsense mediated mRNA degradation (NMD) pathway, but it also regulates various cellular processes, including gene expression quality control and stress response.

Function	Description
NMD path execution	Identify and degrade mrnas containing prematurely terminated codons to prevent the generation of erroneous proteins.
UPF1 dephosphorylation regulation	It forms a complex with SMG7, regulates the phosphorylation state of UPF1, and determines the degradation fate of mRNA.
Fine regulation of gene expression	By selectively degrading specific mrnas, it affects the gene expression patterns of the developmental, immune and nervous systems.
Cellular stress response	Regulate the stability of stress-related mRNA under oxidative stress and DNA damage conditions.
Defense against virus infection	Degrade viral RNA and participate in antiviral immune responses.
Tumor suppression	By eliminating mutant transcripts, genomic stability is maintained, and its functional loss is associated with a variety of cancers

The interaction between SMG5 and SMG7 shows a synergistic effect, which is different from the linear action mode of a single factor, indicating that it plays a key regulatory node role in the NMD pathway. Its abnormal function can lead to developmental defects and the occurrence of diseases, highlighting its importance in cell quality control.

Applications of SMG5 and SMG5 Antibody in Literature

1. Boehm, Volker, et al. "SMG5-SMG7 authorize nonsense-mediated mRNA decay by enabling SMG6 endonucleolytic activity." Nature communications 12.1 (2021): 3965. https://doi.org/10.1038/s41467-021-24046-3

Research has found that SMG5 has an independent function in the NMD pathway and can replace SMG7 to activate mRNA degradation. There is a functional association between the degradation branches of SMG5-SMG7 and SMG6. Either of them can support the endonuclease activity of SMG6, revealing a new mechanism of two-factor authentication in the terminal step of NMD.

2. Wang, Yu, et al. "Overexpression of TMEM79 combined with SMG5 is related to prognosis, tumor immune infiltration and drug sensitivity in hepatocellular carcinoma." European Journal of Medical Research 28.1 (2023): 490. https://doi.org/10.1186/s40001-023-01388-w

Research has found that SMG5 and TMEM79 are co-highly expressed in hepatocellular carcinoma (HCC), jointly influencing the prognosis of patients. Both are related to tumor immune infiltration, immune checkpoints and drug sensitivity, and may serve as potential immunotherapy targets and independent prognostic markers for HCC.

3. Chen, Chengyan, et al. "RNA Surveillance Factor SMG5 Is Essential for Mouse Embryonic Stem Cell Differentiation." Biomolecules 14.8 (2024): 1023. https://doi.org/10.3390/biom14081023

Research has found that the absence of SMG5 leads to the early death of mouse embryos (before E13.5), but embryonic stem cells can still survive. Studies have found that SMG5 affects the differentiation process of stem cells by regulating the protein level of c-MYC and the expression of splicing factors, revealing the key role of the SMG5-NMD pathway in cell state transition.

4. Yi, et al. "MicroRNA 433 regulates nonsense-mediated mRNA decay by targeting SMG5 mRNA." BMC Molecular Biology 17.1 (2016): 17. https://doi.org/10.1186/s12867-016-0070-z

Studies have found that miR-433 inhibits the expression of SMG5 mRNA by targeting its 3'-UTR, thereby weakening the activity of nonsense mediated mRNA degradation (NMD). The down-regulation of SMG5 leads to the accumulation of NMD substrates TBL2 and GADD45B, revealing a new mechanism by which miRNA regulates the NMD pathway.

5. Zhang, Yi, et al. "The m6A demethylase ALKBH5-mediated upregulation of DDIT4-AS1 maintains pancreatic cancer stemness and suppresses chemosensitivity by activating the mTOR pathway." Molecular cancer 21.1 (2022): 174. https://doi.org/10.1186/s12943-022-01647-0

Research has found that in pancreatic cancer, ALKBH5 up-regulates the expression of DDIT4-AS1 through m6A modification. This lncRNA enhances tumor stemness and gemcitabine resistance by hindering the binding of SMG5 and PP2A to UPF1, promoting the phosphorylation of UPF1. Targeting this pathway may improve chemotherapy resistance in pancreatic cancer.

Creative Biolabs: SMG5 Antibodies for Research

Creative Biolabs specializes in the production of high-quality SMG5 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

CustomSMG5 Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our SMG5 antibodies, custom preparations, or technical support, contact us at email.

Reference

Boehm, Volker, et al. "SMG5-SMG7 authorize nonsense-mediated mRNA decay by enabling SMG6 endonucleolytic activity." Nature communications 12.1 (2021): 3965. https://doi.org/10.1038/s41467-021-24046-3