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The specific autophagosomal localization of both WIPI1 and WIPI2 (显示 WIPI2 蛋白) (refered to as WIPI puncta) has been employed to assess autophagy using fluorescence microscopy methods, such as confocal and live-cell video microscopy
Data suggest WIPI1/WIPI2 co-localize with microtubule-associated light chain 3 and autophagy related proteins 2/14L, participate in biogenesis of phagosomes, autophagy, and mobilization of lipids to/from intracellular droplets. [review-like article]
WIPI-1 and WIPI-2 (显示 WIPI2 蛋白) are functionally required in mediating the PI3P signal at the onset of autophagy in NB4 cells.
the detection of WIPI1 mRNA is likely to be a convenient method of monitoring autophagosome formation in a wide range of cell types
Freeze-fracture replica immunolabelling reveals WD-repeat protein (显示 DCAF7 蛋白) interacting with phosphoinositides 1 and 2 (WIPI-1 and WIPI-2 (显示 WIPI2 蛋白)) as membrane components of autophagosomes and the plasma membrane (PM).
Studies define a distinct role for WIPI1 and TORC1 (显示 CRTC1 蛋白) signaling in controlling the transcription of melanogenic enzymes and melanosome maturation, a process that is distinct from starvation-induced autophagy.
Quantification of WIPI-1 puncta should be suitable to assay mammalian autophagy
WD40 repeat proteins are key components of many essential biologic functions. They regulate the assembly of multiprotein complexes by presenting a beta-propeller platform for simultaneous and reversible protein-protein interactions. Members of the WIPI subfamily of WD40 repeat proteins, such as WIPI1, have a 7-bladed propeller structure and contain a conserved motif for interaction with phospholipids (Proikas-Cezanne et al., 2004
WD repeat domain phosphoinositide-interacting protein 1
, WD40 repeat protein Interacting with phosphoInositides of 49kDa
, WD40 repeat protein interacting with phosphoinositides of 49 kDa
, WIPI 49 kDa
, WIPI-1 alpha
, atg18 protein homolog
, WD repeat domain, phosphoinositide interacting 1
, WD repeat domain phosphoinositide-interacting protein 1-like
, WD repeat domain, phosphoinositide-interacting 1