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WDFY3 encodes a phosphatidylinositol 3-phosphate-binding protein that functions as a master conductor for aggregate clearance by autophagy. Additionally we are shipping WDFY3 Antibodies (68) and and many more products for this protein.
we demonstrate that normally ALFY attenuates the canonical Wnt (show WNT2 ELISA Kits) signaling pathway via autophagy-dependent removal specifically of aggregates of DVL3 (show DVL3 ELISA Kits) and not of Dvl1 (show DVL1 ELISA Kits) or Dvl2 (show DVL2 ELISA Kits).
ALFY binds selectively to LC3C and the GABARAPs through a LC3 (show MAP1LC3A ELISA Kits)-interacting region in its WD40 domain (show DCAF12L2 ELISA Kits).
increasing Alfy-mediated protein degradation may be beneficial in some organs, but may be detrimental in others
Data suggest that p62 (show GTF2H1 ELISA Kits) and ALFY interact to organize misfolded, ubiquitinated proteins into protein bodies that become degraded by autophagy.
The selective macroautophagic degradation of aggregated proteins requires the PI3P-binding protein Alfy.
Alfy might target cytosolic protein aggregates for autophagic degradation.
Data provide a novel association between WDFY3 and the RANKL (show TNFSF11 ELISA Kits)-induced osteoclastogenesis pathway via the modulation of TRAF6 (show TRAF6 ELISA Kits).
Alfy translocalization likely is involved in the pathogenesis of amyotrophic lateral sclerosis.
Wdfy3 is important in regulating neural progenitor divisions, neural migration, cerebral expansion and functional organization in the developing brain. Loss-of-function leads to pathological changes characteristic of autism spectrum disorders.
gene expression profiling; in situ hybridization analysis revealed that the expressed BWF1 mRNA was restricted to the marginal region both in E14 and E16 (show SLC7A5 ELISA Kits) embryonic brain, but became diffuse after birth
This gene encodes a phosphatidylinositol 3-phosphate-binding protein that functions as a master conductor for aggregate clearance by autophagy. This protein shuttles from the nuclear membrane to colocalize with aggregated proteins, where it complexes with other autophagic components to achieve macroautophagy-mediated clearance of these aggregated proteins. However, it is not necessary for starvation-induced macroautophagy.
WD repeat and FYVE domain containing 3
, WD repeat and FYVE domain-containing protein 3
, autophagy-linked FYVE protein
, beach domain, WD repeat and FYVE domain-containing protein 1
, galactosyltransferase 3 beta 1, 4