ENSA Antibodies

Background

ENSA is a small molecule protein widely present in eukaryotic cells, mainly involved in the dynamic regulation and signal transduction processes of the cytoskeleton. This protein plays a key role in maintaining the structural stability and polarity of cells by binding to α -adductor proteins, regulating the morphological changes of cell membranes and cell migration. ENSA was first discovered in 1996. Its unique phosphorylation regulatory mechanism - particularly through the activation pathway mediated by Greatwall kinase in the cell cycle - provides important clues for understanding the precise regulation of mitosis. As a specific inhibitor of PP2A phosphatase, the crystal structure analysis of ENSA and the study of its interaction with the B55 regulatory subunit have greatly promoted the progress in the fields of cell cycle regulation and cancer therapeutic targets. Its molecular mechanism has become one of the important research models in modern cell biology.

Structure Function Application Advantage Our Products

Structure of ENSA

ENSA is a small regulatory protein with a molecular weight of approximately 15-18 kDa, and its precise molecular weight varies slightly depending on species and post-translational modifications.

Species	Human	Mice	Fruit flies	Yeast
Molecular Weight (kDa)	17.2	17.0	16.8	15.6
Primary Structural Differences	Containing conserved phosphorylation site (Ser67)	Highly homologous to humans	Simplify the regulatory structure	No PP2A inhibition function

ENSA is composed of 136 amino acids and has a compact spherical structure, with its core made up of β -folds and short α -helices. The protein surface contains a highly conserved phosphorylation site (Ser67), which, upon phosphorylation by Greatwall kinase, triggers a conformational change, enabling it to bind to and inhibit the PP2A-B55 phosphatase complex. The activity regulation of ENSA depends on the cell cyclin-dependent phosphorylation/dephosphorylation cycle. The hydrophobic core in its tertiary structure maintains stability, while the flexible loop participates in specific interactions. This protein has maintained the conservation of its core functional regions during evolution, but it may exhibit adaptive differentiation of regulatory mechanisms in different species.

Fig. 1:Changes in the structure of ENSA. (OA Literature) Fig. 1 ENSA Amplification Drives TNBC Progression via STAT3-SREBP2 Cholesterol Biosynthesis Axis.¹

Key structural properties of ENSA:

Conservative β -folded core structure
Variable N/ C-terminal control region
PP2A-B55 inhibitory domain
Phosphorylation-dependent switching mechanism

Functions of ENSA

The core function of ENSA is to regulate the cell cycle process and participate in a variety of key cellular physiological processes simultaneously.

Function	Description
PP2A phosphatase inhibition	After phosphorylation, it specifically inhibits the PP2A-B55 complex, maintaining the phosphorylation state of key mitotic proteins.
Cell cycle regulation	G2/M phase transition is controlled through CDK1-Greatwal-ENSA pathway to ensure correct chromosome segregation.
Maintenance of genomic stability	Prevent premature exit from mitosis and reduce the production of aneuploid cells.
Stress response	Regulating repair pathways during DNA damage and influencing cell fate determination (repair/apoptosis).
Establishment of cell polarity	Synergistic with cytoskeleton, involved in asymmetric division and cell differentiation.

The activity regulation of ENSA exhibits bistable switch characteristics (phosphorylation activation/dephosphorylation inactivation), which forms a dynamic balance with the sustained activity of PP2A. This precise regulatory mechanism is crucial for the timing control of the cell cycle. Its dysfunction is closely related to various pathological processes such as cancer and neurodegenerative diseases.

Applications of ENSA and ENSA Antibody in Literature

1. Chen, Yi-Yu, et al. "Copy number amplification of ENSA promotes the progression of triple-negative breast cancer via cholesterol biosynthesis." Nature communications 13.1 (2022): 791. https://doi.org/10.1038/s41467-022-28452-z

The article indicates that the ENSA gene in the 1q21.3 region is frequently amplified and highly expressed in TNBC, promoting cholesterol synthesis and driving tumor progression by activating the STAT3/SREBP2 pathway. STAT3 inhibitors are effective against TNBC with high expression of ENSA, and ENSA antibodies may become potential targets.

2. Charrasse, Sophie, et al. "Ensa controls S-phase length by modulating Treslin levels." Nature communications 8.1 (2017): 206. https://doi.org/10.1038/s41467-017-00339-4

The article indicates that ENSA knockout prolongs the S phase by reducing the replication fork density, and the mechanism is that the Gwl/Ensa pathway regulates the ubiquitin-proteasome degradation of Treslin. Overexpression of Treslin can salvage the prolonged S phase, suggesting that ENSA antibodies can be used to study cell cycle regulation.

3. Ysselstein, Daniel, et al. "Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity." Acta neuropathologica communications 5.1 (2017): 3. https://doi.org/10.1186/s40478-016-0403-7

The article indicates that ENSA exerts neuroprotective effects by inhibiting the oligomerization of membrane-bound α -synuclein (aSyn). Research has found that the expression of ENSA is down-regulated in the brains of patients with synuclein, and its antibodies may become potential targets for the treatment of neurodegenerative diseases.

4. Hégarat, Nadia, et al. "PP2A/B55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit." PLoS genetics 10.1 (2014): e1004004. https://doi.org/10.1371/journal.pgen.1004004

The article indicates that ENSA/ARPP19, as a substrate of Greatwall kinase, regulates the activity of PP2A/B55 through phosphorylation and affects the mitotic process. Research has found that Fcp1 phosphatase specifically dephosphorylates ENSA, and its antibody can be used to monitor cell cycle dynamics.

5. Gouttia, Odjo G., et al. "The MASTL-ENSA-PP2A/B55 axis modulates cisplatin resistance in oral squamous cell carcinoma." Frontiers in cell and developmental biology 10 (2022): 904719.https://doi.org/10.3389/fcell.2022.904719

The article indicates that the MASTL-ENSA/PP2A-B55 pathway regulates cisplatin resistance in oral squamous cell carcinoma. Studies have found that overexpression of ENSA-dependent MASTL promotes tumor survival, while the absence of ENSA or overexpression of B55α can enhance cisplatin sensitivity, suggesting that ENSA antibodies can be used for research on drug resistance mechanisms and treatment evaluation.

Creative Biolabs: ENSA Antibodies for Research

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

Custom ENSA 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 ENSA antibodies, custom preparations, or technical support, contact us at email.

Reference

Chen, Yi-Yu, et al. "Copy number amplification of ENSA promotes the progression of triple-negative breast cancer via cholesterol biosynthesis." Nature communications 13.1 (2022): 791. https://doi.org/10.1038/s41467-022-28452-z