SUMOylation of proteins plays a key role in modulating neuronal function. For this reason, the balance between protein SUMOylation and deSUMOylation requires fine regulation to guarantee the homeostasis of neural tissue. While extensive research has been carried out on the localization and function of small ubiquitin-related modifier (SUMO) variants in neurons, less attention has been paid to the SUMO-specific isopeptidases that constitute the human SUMO-specific isopeptidase (SENP)/Ubiquitin-Specific Protease (ULP) cysteine protease family (SENP1-3 and SENP5-7). Here, for the first time, we studied the localization of SENP1, SENP6, and SENP7 in cultured hippocampal primary neurons at a super resolution detail level, with structured illumination microscopy (SIM). We found that the deSUMOylases partially colocalize with pre-and post-synaptic markers such as synaptophysin and drebrin. Thus, further confirming the presence with synaptic markers of the negative regulators of the SUMOylation machinery.
Neuronal Localization of SENP Proteins with Super Resolution Microscopy / L. Colnaghi, A. Conz, L. Russo, C.A. Musi, L. Fioriti, T. Borsello, M. Salmona. - In: BRAIN SCIENCES. - ISSN 2076-3425. - 10:11(2020 Nov).
|Titolo:||Neuronal Localization of SENP Proteins with Super Resolution Microscopy|
|Parole Chiave:||SENPs; SUMO; neurons; super resolution microscopy;|
|Settore Scientifico Disciplinare:||Settore BIO/16 - Anatomia Umana|
|Data di pubblicazione:||nov-2020|
|Data ahead of print / Data di stampa:||25-ott-2020|
|Digital Object Identifier (DOI):||http://dx.doi.org/10.3390/brainsci10110778|
|Appare nelle tipologie:||01 - Articolo su periodico|