AMOT Antibodies

Background

AMOT is a scaffold protein, mainly expressed in endothelial cells and epithelial cells of vertebrates. The protein encoded by this gene plays a key role in embryonic development and the maintenance of tissue homeostasis by participating in processes such as cell polarity establishment, cell migration and angiogenesis. It is particularly worth noting that AMOT can interact with the core components of the Hippo signaling pathway, thereby regulating organ size and tumor suppressive function. Scientists first identified the AMOT gene in 2003. Subsequent research has found that its abnormal expression is closely related to various cancers and vascular diseases. As an important component of cell junction complexes, AMOT has become a hot topic in cell biology and oncology research due to its unique molecular mechanism, providing a new perspective for understanding tissue morphogenesis and cancer metastasis.

Structure Function Application Advantage Our Products

Structure of AMOT

Myoglobin is a relatively small protein with a molecular weight of approximately 16.7 kDa. This weight may slightly vary between species due to minor differences in amino acid sequence.

Species	Human	Mouse	Rat	Zebrafish
Molecular Weight (kDa)	~100 (AMOT p130)	~98 (AMOT p130)	~100 (AMOT p130)	~85 (homologous gene)
Primary Structural Differences	Containing PPxY motif, PDZ binding domain	Highly conservative and functionally similar	Highly homologous to human AMOT	Retain the regulatory function of the Hippo pathway

The AMOT protein is composed of multiple functional domains, including the n-terminal coiled-coil domain, the intermediate PDZ binding domain, and the c-terminal PPxY motif. These structures enable it to interact with various signaling molecules, such as YAP/TAZ and LATS kinases. Its tertiary structure forms a stable scaffold, participates in the assembly of cell junction complexes, and plays a key role in cell polarity, migration and angiogenesis. The subcellular localization of AMOT (such as in the cell membrane or cytoplasm) is regulated by phosphorylation, which affects its functional activity.

Fig. 1:Changes in the structure of AMOT. Fig. 1 Domain architecture of Amot protein. ¹

Key structural properties of AMOT:

Multi-domain scaffold protein
Hippo pathway regulatory core
Phosphorylation-dependent functional regulation
Cell junction localization

Functions of AMOT

The core function of the AMOT gene is to regulate cell polarity and migration, and it is also involved in a variety of physiological and pathological processes, including angiogenesis, tumor suppression and mechanical signal transduction.

Function	Description
Establishment of cell polarity	By connecting the cell membrane with the cytoskeleton, it regulates the apical and basal polarity of epithelial cells and endothelial cells, maintaining the function of the tissue barrier.
Hippo pathway regulation	As a key inhibitor of YAP/TAZ, it inhibits excessive cell proliferation and tumorigenesis through LATS kinase-dependent phosphorylation.
Angiogenesis regulation	By integrating VEGF and Angiopoietin signals, endothelial cell migration and vascular lumen formation are controlled, influencing embryonic development and wound repair.
Mechanical force induction	In response to changes in extracellular matrix hardness, mechanical signals are transmitted through cell junction complexes (such as tight junctions) to regulate cell morphology and migration.
Tumor metastasis inhibition	In various cancers (such as breast cancer and liver cancer), the absence of AMOT expression can lead to the activation of YAP, promoting tumor invasion and metastasis.

The functional exertion of AMOT depends on its subcellular localization (such as at cell junctions or in the cytoplasm) and phosphorylation status. Its mechanism of action is more complex than that of traditional scaffold proteins and involves cross-regulation of multiple signaling pathways.

Applications of AMOT and AMOT Antibody in Literature

1. Rojek, Katarzyna O., et al. "Amot and Yap1 regulate neuronal dendritic tree complexity and locomotor coordination in mice." PLoS biology 17.5 (2019): e3000253.https://doi.org/10.1371/journal.pbio.3000253

Research has found that angioactin (Amot) and Hippo pathway co-activator Yap1 jointly promote the dendrite development of hippocampal neurons and Purkinje cells by regulating the phosphorylation of S6 kinase (rather than TEAD transcription factors), and their absence can lead to abnormal cerebellar morphology and motor coordination disorders.

2. Rheinemann, Lara, et al. "Interactions between AMOT PPxY motifs and NEDD4L WW domains function in HIV-1 release." Journal of Biological Chemistry 297.2 (2021). https://doi.org/10.1016/j.jbc.2021.100975

Research has found that the HIV virus binds with high affinity to the WW3 domain of NEDD4L through the PPxY1 motif of the AMOT protein, promoting the formation and release of the viral envelope. Among them, ionic and hydrophobic interactions are the key mechanisms.

3. Jiang, Lai, et al. "Cell size regulates human endoderm specification through actomyosin-dependent AMOT-YAP signaling." Stem Cell Reports 19.8 (2024): 1137-1155.https://doi.org/10.1016/j.stemcr.2024.07.001

Research has found that when human stem cells differentiate into the endoderm, the cell volume decreases. Hypertonic pressure promotes AMOT nuclear translocation by activating actibulin and inhibits YAP activity, thereby enhancing endoderm differentiation.

4. Heller, Brigitte, et al. "Amot recognizes a juxtanuclear endocytic recycling compartment via a novel lipid binding domain." Journal of Biological Chemistry 285.16 (2010): 12308-12320. https://doi.org/10.1074/jbc.m109.096230

Research has found that the polar protein Amot specifically recognizes phosphatidylinositol monophosphate and cholesterol through a novel lipid-binding domain, mediating the translocation of the Patj/Mupp1 complex from the plasma membrane to the systemic circulation compartment, thereby regulating cell polarity.

5. Zhu, Guoqing, et al. "12-O-Tetradecanoylphorbol-13-acetate (TPA) is anti-tumorigenic in liver cancer cells via inhibiting YAP through AMOT." Scientific reports 7.1 (2017): 44940.https://doi.org/10.1038/srep44940

Research has found that TPA promotes the translocation of YAP from the nucleus to the cytoplasm through an AmOT-dependent mechanism, blocking its transcriptional activity and thereby inhibiting the malignant phenotype of liver cancer cells. The absence of AMOT will eliminate the anti-tumor effect of TPA, indicating that the AMOT-YAP axis is the key pathway for TPA to exert its tumor suppression function.

Creative Biolabs: AMOT Antibodies for Research

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

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

Reference

Rojek, Katarzyna O., et al. "Amot and Yap1 regulate neuronal dendritic tree complexity and locomotor coordination in mice." PLoS biology 17.5 (2019): e3000253.https://doi.org/10.1371/journal.pbio.3000253