The Vps4 C-terminal helix is a critical determinant for assembly and ATPase activity and has elements conserved in other members of the meiotic clade of AAA ATPases.

Vajjhala, P. R., Nguyen , C. H., Landsberg, M. J., Kistler, C., Gan, A. L., King, G. F., Hankamer, B. and Munn, A. L. (2008) The Vps4 C-terminal helix is a critical determinant for assembly and ATPase activity and has elements conserved in other members of the meiotic clade of AAA ATPases.. Febs Journal, 275 7: 1427-1449. doi:10.1111/j.1742-4658.2008.06300.x


Author Vajjhala, P. R.
Nguyen , C. H.
Landsberg, M. J.
Kistler, C.
Gan, A. L.
King, G. F.
Hankamer, B.
Munn, A. L.
Title The Vps4 C-terminal helix is a critical determinant for assembly and ATPase activity and has elements conserved in other members of the meiotic clade of AAA ATPases.
Journal name Febs Journal   Check publisher's open access policy
ISSN 1742-464X
1742-4658
Publication date 2008-01-16
Year available 2008
Sub-type Article (original research)
DOI 10.1111/j.1742-4658.2008.06300.x
Volume 275
Issue 7
Start page 1427
End page 1449
Total pages 22
Editor G. D. Foster
Place of publication United Kingdom
Publisher Wiley-Blackwell
Collection year 2009
Language eng
Subject C1
270403 Plant Pathology
970106 Expanding Knowledge in the Biological Sciences
Abstract Sorting of membrane proteins into intralumenal endosomal vesicles, multivesicular body (MVB) sorting, is critical for receptor down regulation, antigen presentation and enveloped virus budding. Vps4 is an AAA ATPase that functions in MVB sorting. Although AAA ATPases are oligomeric, mechanisms that govern Vps4 oligomerization and activity remain elusive.
Keyword endocytosis
lysosome
macromolecular
complex
membrane traffic
Vacuole
Q-Index Code C1
Q-Index Status Confirmed Code

 
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Created: Tue, 07 Apr 2009, 12:19:55 EST by Cody Mudgway on behalf of Institute for Molecular Bioscience