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WD40 repeat proteins are key components of many essential biologic functions. Additionally we are shipping WIPI2 Antibodies (82) and many more products for this protein.
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Here the authors show that recruitment of WIPI2, itself essential for anti-bacterial autophagy, is dependent on the localization of catalytically active TBK1 (show TBK1 Proteins) to the vicinity of cytosolic bacteria.
The specific autophagosomal localization of both WIPI1 (show WIPI1 Proteins) and WIPI2 (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 (show WIPI1 Proteins) 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 (show WIPI1 Proteins) and WIPI-2 are functionally required in mediating the PI3P signal at the onset of autophagy in NB4 cells.
Data suggest that WIPI2b directly interacts with dimer of ATG16L1 (autophagy related 16-like 1 (show ATG16L1 Proteins)) and this interaction is linked to production of phosphatidylinositol 3-phosphate in endoplasmic reticulum triggered by autophagosome formation. [REVIEW]
WIPI2b binds the membrane surrounding Salmonella and recruits the Atg12 (show ATG12 Proteins)-5-16L1 complex, initiating LC3 (show MAP1LC3A Proteins) conjugation, autophagosomal membrane formation, and engulfment of Salmonella.
WIPI2 is a phosphatidylinsitol-3-phosphate binding protein required for starvation induced autophagy.
Freeze-fracture replica immunolabelling reveals WD-repeat protein (show DCAF7 Proteins) interacting with phosphoinositides 1 and 2 (WIPI-1 (show WIPI1 Proteins) and WIPI-2) as membrane components of autophagosomes and the plasma membrane (PM).
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 WIPI2, 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 2
, WD40 repeat protein interacting with phosphoinositides 2
, WIPI49-like protein 2