Rho GTPase-activating protein 35 (ARHGAP35)

Rho GTPase-activating protein 35 (ARHGAP35) is a critical enzyme involved in signal transduction from Rho-family GTPases, primarily serving to inactivate RhoA and Rac1 through its GAP domain. It participates in the regulation of actin cytoskeleton remodeling, cell adhesion, migration, cell division, and has key roles in the development of retinal tissue, neural tube, and renal structures. ARHGAP35 is also implicated in the regulation of transcription and gene expression, interacting with transcription factors and repressing glucocorticoid receptor transcription. Loss-of-function mutations in ARHGAP35 are associated with developmental disorders affecting the eye and neural tissue, and it is functionally characterized as a tumor suppressor in several cancer types. ARHGAP35 contains several functional domains—GAP (GTPase-activating), pseudo-GTPase, FF, and leucine zipper-like—allowing diverse regulatory and structural interactions. Germline and somatic mutations often cluster in the catalytic GAP domain, underscoring its importance in health and disease.

Other names

GRLF1 (Glucocorticoid receptor DNA-binding factor 1)p190Ap190ARhoGAPGRF1KIAA1722p190-RhoGAPGlucocorticoid receptor repression factor 1

Not applicable—no direct inhibitors/modulators reported. Mechanisms for potential future drugs would likely involve: - Modulation of GAP activity (enhancement/restoration of tumor suppressor function) - Modulation of RhoA/Rac1 activity downstream