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AMOT belongs to the motin family of angiostatin binding proteins characterized by conserved coiled-coil domains and C-terminal PDZ binding motifs. Additionally we are shipping Angiomotin Antibodies (98) and Angiomotin Kits (16) and many more products for this protein.
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Amot and AmotL1 have similar effects on endothelial migration and tight junction formation in vitro. In vivo Amot appears to control the cell polarity and AmotL1 affects the stability of cell-cell junctions.
Thus AMOT is a direct substrate of Lats1/2 mediating functions of the Hippo pathway in endothelial cell migration and angiogenesis.
knockdown of Amot reduced the number of filopodia of endoth (show PDPN Proteins)elial tip cells and severely impaired the migration of intersegmental vessels
angiomotin and Merlin respectively interface cortical actin filaments and core kinases in Hippo signaling
Study shows miR (show MLXIP Proteins)-205 significantly downregulated and directly target the 3'-UTR of AMOT in breast cancer. In vitro, miR (show MLXIP Proteins)-205 regulates the proliferation and invasion of breast cancer cells through suppression of AMOT expression.
Amot was highly expressed in breast cancer tissues and was important in the promotion of breast cancer cell proliferation and invasion. Amot knockdown in MCF-7 cells decreased the expression of YAP, YAP/TAZ and LATS1.
experiments indicate that AMOT and other motin family members function together with NEDD4L (show NEDD4L Proteins) to help complete immature virion assembly prior to ESCRT-mediated virus budding
AMOT is a crucial suppressor of lung cancer metastasis and highlight its critical role as a tumor suppressor and its potential as a prognostic biomarker and therapeutic target for lung cancer.
angiomotin proteins connect F-actin architecture to YAP (show YAP1 Proteins) regulation.
Scaffold proteins angiomotin (Amot) and angiomotin-related AmotL1 and AmotL2 (show AMOTL2 Proteins) were recently identified as negative regulators of YAP (show YAP1 Proteins) and TAZ (show TAZ Proteins) by preventing their nuclear translocation.
Within the nucleus, Amot-p130 (show RBL2 Proteins) was associated with the transcriptional complex containing Yap (show YAP1 Proteins) and Teads (TEA domain family members) and contributed to the regulation of a subset of Yap (show YAP1 Proteins) target genes, many of which are associated with tumorigenesis.
These results collectively suggest that the Hippo pathway negatively regulates the actin-binding activity of Amot family members through direct phosphorylation.
Within the nucleus, Amot-p130 was associated with the transcriptional complex containing Yap (show YAP1 Proteins) and Teads (TEA domain family members) and contributed to the regulation of a subset of Yap (show YAP1 Proteins) target genes, many of which are associated with tumorigenesis.
The loss of Angiomotin, together with Angiomotin-like 2 (show AMOTL2 Proteins), leads to differentiation of inner cell mass cells and compromised peri (show POSTN Proteins)-implantation development.
The phosphorylation of S176 in the N-terminal domain of Amot is a critical step for activation of the Hippo pathway in adherens junctions and cell polarity disconnects the Hippo pathway from cell-cell adhesion by sequestering Amot from AJs.
Amot, Amotl1, and Amotl2 (show AMOTL2 Proteins) are differentially expressed in uterine cells during the peri (show POSTN Proteins)-implantation period.
A vaccine targeting angiomotin induces an antibody response which alters tumor vessel permeability and hampers the growth of established tumors.
Depletion of Angiomotin in Nf2 (show NF2 Proteins)(-/-) Schwann cells attenuates the Ras-MAPK (show MAPK1 Proteins) signaling pathway, impedes cellular proliferation in vitro and tumorigenesis in vivo
Angiomotin may promote neoplastic angiogenesis by both stimulating invasion as well as stabilizing established tubes.
angiomotin, in addition to controlling cell motility, may play a role in the assembly of endothelial cell-cell junctions
p80 (show COIL Proteins)- and p130-angiomotin play coordinating roles in vascular tube formation by affecting cell migration and cell shape, respectively.
This gene belongs to the motin family of angiostatin binding proteins characterized by conserved coiled-coil domains and C-terminal PDZ binding motifs. The encoded protein is expressed predominantly in endothelial cells of capillaries as well as larger vessels of the placenta where it may mediate the inhibitory effect of angiostatin on tube formation and the migration of endothelial cells toward growth factors during the formation of new blood vessels. Alternative splicing results in multiple transcript variants encoding different isoforms.
angiomotin like 2
, angiomotin-like protein 2
, angiomotin-like protein 2-like
, angiomotin p130 isoform
, angiomotin p80 isoform