...Qiong Lin; Qian Dai; Hongxia Meng; Aiqin Sun; Jing Wei; Ke Peng; Chandra Childress; Miao Chen; Genbao Shao; Wannian Yang ABSTRACT Our previous studies have shown that the HECT E3 ubiquitin ligase NEDD4 interacts with LC3 and is required for starvation and rapamycin-induced activation of autophagy...

... phosphorylation-dependent changes in accessibility of key RET9 C-terminal binding motifs that facilitate interactions with multiple adaptor proteins, including GRB10 and SHANK2, to recruit the NEDD4 ubiquitin ligase. We showed that NEDD4-mediated ubiquitylation is required for RET9 localization to clathrin-coated...

..., resulting in loss of gap junctions. However, the molecular basis underlying the aberrant regulation of Cx43 in cancer cells has remained elusive. Here, we demonstrate that the oncogenic E3 ubiquitin ligase NEDD4 regulates the Cx43 protein level in HeLa cells, both under basal conditions and in response...

... a small siRNA screen, we highlighted two additional regulators of BST2 constitutive ubiquitylation and sorting to the lysosomes: the E3 ubiquitin ligases NEDD4 and MARCH8. Interestingly, Vpu does not hijack the cellular machinery that is constitutively involved in BST2 ubiquitylation to sort BST2...

... that mediate initial contact and subsequent maturation of cell–cell junctions. Here we report that Rac1 associates with the ubiquitin–protein ligase neural precursor cell expressed developmentally down-regulated 4 (Nedd4). This interaction requires the hypervariable C-terminal domain of Rac1 and the WW domains...

...Linda M. Shearwin-Whyatt; Darren L. Brown; Fiona G. Wylie; Jennifer L. Stow; Sharad Kumar N4WBP5A (Ndfip2) belongs to an evolutionarily conserved group of Nedd4-interacting proteins with two homologues in mammalian species. We have previously shown that N4WBP5A expression in Xenopus oocytes results...

...Natalia Shcherbik; Sharad Kumar; Dale S. Haines Mammalian Nedd4 and its budding yeast orthologue Rsp5 are members of a large family of HECT-domain-containing ubiquitin ligases. Besides possessing a Ca 2+ /lipid-binding domain, both ligases have multiple protein-interacting modules termed WW domains...