Identification of novel interacting partners of the NEDD4 ubiquitin ligase in mouse testis
JantinaA Manning, Simon P Windley, Jarrod J Sandow, Sonia S Shah, Patrick Western, Dagmar Wilhelm, Sharad Kumar
Journal of Proteomics | ELSEVIER | Published : 2020
Posttranslational modification by ubiquitination targets proteins for degradation, recycling, stabilization or altered trafficking, and as such can alter cellular signaling pathways. The substrate specificity of this multistep process is controlled by ubiquitin ligases, including those of the HECT domain-containing NEDD4 family. In the testis, ubiquitination of many proteins contributes to organ development and maturation of spermatozoa and NEDD4 is known to be important in the control of spermatogonial stem cell homeostasis. However, a comprehensive understanding of NEDD4 substrates in testis development is lacking. Here we demonstrate high expression of Nedd4 in somatic cells of the mouse ..View full abstract
Awarded by Australian Research Council
Awarded by National Health and Medical Research Council Senior Principal Research Fellowship
This work was supported by an Australian Research Council Discovery Grant (150101448) to D.W and S.K., a National Health and Medical Research Council Senior Principal Research Fellowship (1103006) and a University of South Australia Support Package to S.K. We thank Andrej Nikolic for help with cloning of GFP-tagged NEDD4 and the University of Melbourne's Biological Optical Microscopy Platform for use of their confocal microscope. Mass spectrometry and proteomics analysis were conducted within the laboratory of Andrew Webb at WEHI and supported by the Victorian Government Operational Infrastructure Support scheme.