Function of Torsin AAA+ ATPases in Pseudorabies Virus Nuclear Egress
نویسندگان
چکیده
منابع مشابه
Torsin ATPases: Harnessing Dynamic Instability for Function
Torsins are essential, disease-relevant AAA+ (ATPases associated with various cellular activities) proteins residing in the endoplasmic reticulum and perinuclear space, where they are implicated in a variety of cellular functions. Recently, new structural and functional details about Torsins have emerged that will have a profound influence on unraveling the precise mechanistic details of their ...
متن کاملIdentification of conserved amino acids in pUL34 which are critical for function of the pseudorabies virus nuclear egress complex.
UNLABELLED Nuclear egress of herpesvirus capsids is mediated by a conserved heterodimeric complex of two viral proteins, designated pUL34 and pUL31 in herpes simplex virus and pseudorabies virus (PrV). pUL34, a tail-anchored membrane protein, is targeted to the nuclear envelope and recruits pUL31 to the inner nuclear membrane (INM) to provide the docking and envelopment machinery for the nascen...
متن کاملA physical link between the pseudorabies virus capsid and the nuclear egress complex.
Following their assembly, herpesvirus capsids exit the nucleus by budding at the inner nuclear membrane. Two highly conserved viral proteins are required for this process, pUL31 and pUL34. In this report, we demonstrate that the pUL31 component of the pseudorabies virus nuclear egress complex is a conditional capsid-binding protein that is unmasked in the absence of pUL34. The interaction betwe...
متن کاملAAA-ATPases in Protein Degradation
Proteolytic machineries containing multisubunit protease complexes and AAA-ATPases play a key role in protein quality control and the regulation of protein homeostasis. In these protein degradation machineries, the proteolytically active sites are formed by either threonines or serines which are buried inside interior cavities of cylinder-shaped complexes. In eukaryotic cells, the proteasome is...
متن کاملRegulation of Torsin ATPases by LAP1 and LULL1.
TorsinA is a membrane-associated AAA+ (ATPases associated with a variety of cellular activities) ATPase implicated in primary dystonia, an autosomal-dominant movement disorder. We reconstituted TorsinA and its cofactors in vitro and show that TorsinA does not display ATPase activity in isolation; ATP hydrolysis is induced upon association with LAP1 and LULL1, type II transmembrane proteins resi...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Cells
سال: 2020
ISSN: 2073-4409
DOI: 10.3390/cells9030738