WD repeat domain phosphoinositide-interacting protein 1 (WIPI1)

WD repeat domain phosphoinositide-interacting protein 1 (WIPI1) is a member of the WD40 repeat protein family, characterized by a beta-propeller structure that facilitates the assembly of multiprotein complexes. WIPI1 functions as a central scaffold and adaptor in autophagy, specifically by binding phosphatidylinositol 3-phosphate and recruiting essential complexes for autophagosome formation and elongation. It collaborates with related proteins to promote lipid transfer and is active in both homeostatic and stress-induced autophagy, mitophagy, xenophagy, and protein trafficking. WIPI1 also influences pigmentation through regulation of melanosome maturation[1][2][3][7][8]. This protein is well-characterized structurally and functionally, and is increasingly studied for its roles in neurodegeneration, cancer, infection responses, and cellular homeostasis. No known nomenclature errors are present; the name and abbreviations are standard across primary databases and literature.

Other names

Atg18 protein homologWD40 repeat protein interacting with phosphoinositides of 49 kDaWIPI49WIPI-1WD repeat domain phosphoinositide interacting 1WIPI 49 kDa

Drugs theoretically targeting WIPI1 would likely modulate autophagy, either by inhibiting or promoting assembly/function of autophagosomes, affecting the degradation of cell material or pathogens