1998
DOI: 10.1016/s0962-8924(97)01212-9
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The AAA team: related ATPases with diverse functions

Abstract: A new family of related ATPases has emerged, characterized by a highly conserved AAA motif. This motif forms a 230-amino-acid domain that contains Walker homology sequences and imparts ATPase activity. Homology between AAA-family members is confined mostly to the AAA domain, although additional homology outside the AAA motif is present among closely related proteins. AAA proteins act in a variety of cellular functions, including cell-cycle regulation, protein degradation, organelle biogenesis and vesicle-media… Show more

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Cited by 442 publications
(357 citation statements)
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“…The structure retains its symmetry and rigidity until all ATP molecules are hydrolyzed, at which point HP0525 can return to its nucleotide free form. Although sequence-unrelated, the structure of HP0525 is remarkably similar to that of the p97 AAA ATPase which, similarly to the related Nethylmaleimide-sensitive fusion protein (NSF), plays a central role in organelle assembly and membrane fusion processes in the endoplasmic reticulum and the Golgi apparatus (Patel and Latterich, 1998;Ye et al, 2001). It has therefore been proposed that VirB11-like proteins, by analogy to p97 and NSF, could serve as mechanical transducers providing the necessary mechanical force for the recruitment/assembly/disassembly of type IV secretion protein components, making them available for insertion into the nascent secretion apparatus and/or to facilitate substrate translocation across the inner membrane (Savvides et al, 2003).…”
Section: Virb11: a Ring-shaped Cytoplasmic Ntpase Fuelling The Secretmentioning
confidence: 99%
“…The structure retains its symmetry and rigidity until all ATP molecules are hydrolyzed, at which point HP0525 can return to its nucleotide free form. Although sequence-unrelated, the structure of HP0525 is remarkably similar to that of the p97 AAA ATPase which, similarly to the related Nethylmaleimide-sensitive fusion protein (NSF), plays a central role in organelle assembly and membrane fusion processes in the endoplasmic reticulum and the Golgi apparatus (Patel and Latterich, 1998;Ye et al, 2001). It has therefore been proposed that VirB11-like proteins, by analogy to p97 and NSF, could serve as mechanical transducers providing the necessary mechanical force for the recruitment/assembly/disassembly of type IV secretion protein components, making them available for insertion into the nascent secretion apparatus and/or to facilitate substrate translocation across the inner membrane (Savvides et al, 2003).…”
Section: Virb11: a Ring-shaped Cytoplasmic Ntpase Fuelling The Secretmentioning
confidence: 99%
“…Vps4p belongs to the ATPases associated with cellular activities (AAA) family of proteins (Babst et al, 1997). Although AAA proteins participate in a wide variety of cellular activities, an emerging theme for their function is in molecular rearrangement and/or unfolding reactions (Confalonieri and Duguet, 1995;Patel and Latterich, 1998;Leonhard et al, 1999). It is possible, therefore, that Vps4p acts to modulate interactions between other components of the vacuolar sorting pathway, including other class E proteins.…”
Section: Localization Of Mammalian Vps4mentioning
confidence: 99%
“…AAA proteins are a group of ATPases that share common sequence features in addition to an ATP-binding motif. These proteins participate in a variety of cellular functions such as cell-cycle regulation, proteolysis, and membrane fusion (Patel and Latterich 1998). Using a positional cloning approach, Fidgetin was identified as the gene causing the inner ear and retinal phenotypes in the spontaneous mouse mutant fidget (Cox et al 2000).…”
Section: Development Of the Semicircular Canalsmentioning
confidence: 99%