AMOT - Angiomotin (like) | Elisa - Clia - Antibody - Protein

Background:

AMOT or Angiomotin is a protein that in humans is encoded by the AMOT gene. Angiomotin is a scaffold protein that plays important roles in various cellular processes, including cell-cell junction formation, cell polarity, and regulation of signaling pathways involved in cell growth and migration. Angiomotin is involved in the assembly and maintenance of tight junctions, adherens junctions, and other cell-cell junctions. These junctions are critical for maintaining the integrity of tissues and regulating the passage of molecules between cells. AMOT is also important for establishing and maintaining cell polarity, which is crucial for the proper functioning of tissues and organs. Cell polarity refers to the asymmetric distribution of cellular components and structures within a cell. Angiomotin interacts with various signaling molecules and pathways to regulate processes such as cell growth, survival, and migration. For example, AMOT can interact with the Hippo signaling pathway, which is involved in controlling organ size and tumor suppression. Angiomotin has also been implicated in angiogenesis, It plays a role in the migration and organization of endothelial cells during blood vessel formation. Dysregulation of Angiomotin has been associated with various cancers. AMOT expression levels can affect the growth and invasive potential of cancer cells. Some studies suggest that AMOT may act as a tumor suppressor in certain contexts, while in others, it may promote cancer progression. Recent research has also suggested roles for Angiomotin in neurological function. For instance, it has been implicated in the development of the nervous system, particularly in the growth and guidance of neuronal processes.

Protein Structure:

• Domains: AMOT contains several key structural domains:
• PDZ-binding motif: This motif at the C-terminal end allows interactions with other proteins containing PDZ domains.
• Coiled-coil domains: These regions are involved in protein-protein interactions, crucial for forming complexes with other proteins.
• LZ (leucine zipper) domain: This domain is important for dimerization and interactions with other proteins.
• PPxY motifs: These motifs interact with WW domain-containing proteins, such as YAP and TAZ, which are critical for the Hippo signaling pathway.

Classification and Subtypes:

• Family: AMOT belongs to the motin family, which includes three members: AMOT (p130), AMOTL1, and AMOTL2.
• Isoforms: AMOT has two main isoforms:
• p130-AMOT: The full-length form, which includes all functional domains.
• p80-AMOT: A shorter isoform lacking the N-terminal half, which includes the first coiled-coil domain but retains the C-terminal PDZ-binding motif.

Function and Biological Significance:

• Angiogenesis: AMOT plays a pivotal role in the regulation of angiogenesis by promoting endothelial cell migration and tube formation, which are essential for new blood vessel formation.
• Cell Migration and Polarity: AMOT is involved in the regulation of cell shape and movement, influencing processes such as wound healing and tissue remodeling.
• Hippo Signaling Pathway: AMOT interacts with YAP/TAZ, key regulators of the Hippo pathway, which controls organ size, cell proliferation, and apoptosis. By binding to YAP/TAZ, AMOT can sequester these transcription co-activators in the cytoplasm, preventing their nuclear translocation and subsequent gene activation.

Interactions:

• YAP/TAZ: AMOT binds to these transcription co-activators, inhibiting their activity by retaining them in the cytoplasm.
• Angiostatin: AMOT interacts with angiostatin, which inhibits endothelial cell migration and angiogenesis.
• VEGF (Vascular Endothelial Growth Factor): AMOT is involved in VEGF-induced angiogenesis, promoting endothelial cell migration and vessel formation.

Clinical Issues:

• Cancer: AMOT is implicated in various cancers, particularly those involving abnormal angiogenesis and cell proliferation. Overexpression or altered regulation of AMOT can contribute to tumor growth and metastasis.
• Liver Regeneration: AMOT plays a role in liver regeneration, with potential implications for liver diseases and transplantation.
• Polycystic Kidney Disease: Altered AMOT function is linked to cyst formation in polycystic kidney disease, affecting kidney function.

Summary:

Angiomotin (AMOT) is a multifunctional protein involved in angiogenesis, cell migration, and the Hippo signaling pathway. Structurally, it features PDZ-binding, coiled-coil, leucine zipper, and PPxY motifs, enabling diverse protein interactions. AMOT is essential for endothelial cell behavior and blood vessel formation, and it regulates the activity of YAP/TAZ in the Hippo pathway. Clinically, AMOT's dysregulation is associated with cancer progression, liver regeneration, and polycystic kidney disease, underscoring its significance in both physiological and pathological contexts.