Angiomotin (AMOT)

Angiomotin (AMOT) is a scaffold protein predominantly expressed in endothelial cells of angiogenic tissues such as the placenta and tumors[1]. It was originally identified as a binding partner of angiostatin and functions to regulate endothelial cell migration, cell–cell junctions, and angiogenesis. AMOT is a member of the motin family (including AMOT, AMOT-like 1, AMOT-like 2) and exists in two principal isoforms (p80 and p130), generated by alternative splicing[1][4][5]. AMOT serves as a scaffold for the Hippo signaling pathway, interacting directly with components such as YAP/TAZ and LATS kinases, thereby regulating organ size, cell proliferation, and tumorigenesis[4][5][6]. Its dysregulation has been implicated in cancer and developmental biology. AMOT does not have canonical enzyme activity, nor is it a receptor or ion channel; rather, it derives its biological importance from organizing multi-protein complexes at cell junctions, influencing proliferation, migration, and tight junction integrity[1][5][6].

Other names

AngiomotinAMOTAngiomotin p80Angiomotin p130

Not a direct drug target; rather, AMOT acts as a scaffold/adaptor for Hippo pathway proteins, influencing YAP/TAZ localization and activity. Some experimental therapeutics modulate AMOT–YAP or AMOT–angiostatin interactions, mainly to affect **angiogenesis** or **tumor growth**.