vasohibinbinding

Vasohibinbinding refers to the molecular interaction between vasohibin proteins (VASH1 and VASH2) and their binding partner SVBP, the vasohibin-binding protein. This interaction is essential for the stability, secretion, and enzymatic activity of vasohibins in endothelial cells, where they influence microtubule dynamics and angiogenesis.

VASH1 and VASH2 are secreted by endothelial cells and have opposing effects on angiogenesis in different contexts. The binding of SVBP to either vasohibin enables the formation of a functional complex that can act as a tubulin carboxypeptidase, promoting detyrosination of alpha-tubulin and thereby modulating microtubule properties. This enzymatic activity is linked to changes in cell migration and vessel formation, which are central to angiogenic regulation.

structurally, SVBP interacts with vasohibin proteins to form a heterodimeric complex. The presence of SVBP stabilizes vasohibin and is generally required for its proper localization and catalytic activity. The vasohibin–SVBP interaction represents a specific protein–protein binding event that integrates signals controlling blood vessel growth.

Regulation of this binding occurs in response to cellular conditions such as hypoxia, signaling cues, and developmental stage, which in turn modulate endothelial behavior and angiogenesis. Dysregulation of vasohibin binding or the VASH-SVBP complex has been implicated in pathological angiogenesis seen in cancer and other diseases.

In research and potential therapy, targeting the vasohibin–SVBP interaction is investigated as a strategy to modulate angiogenesis. Understanding this binding interface helps clarify how tubulin post-translational modifications influence vessel formation and endothelial cell dynamics.