2rkk: Difference between revisions

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==Overview==

The MVB pathway plays essential roles in several eukaryotic cellular, processes. Proper function of the MVB pathway requires reversible membrane, association of the ESCRTs, a process catalyzed by Vps4 ATPase. Vta1, regulates the Vps4 activity, but its mechanism of action was poorly, understood. We report the high-resolution crystal structures of the Did2-, and Vps60-binding N-terminal domain and the Vps4-binding C-terminal domain, of S. cerevisiae Vta1. The C-terminal domain also mediates Vta1, dimerization and both subunits are required for its function as a Vps4, regulator. Emerging from our analysis is a mechanism of regulation by Vta1, in which the C-terminal domain stabilizes the ATP-dependent double ring, assembly of Vps4. In addition, the MIT motif-containing N-terminal domain, projected by a long disordered linker, allows contact between the Vps4, disassembly machinery and the accessory ESCRT-III proteins. This provides, an additional level of regulation and coordination for ESCRT-III assembly, and disassembly.

The MVB pathway plays essential roles in several eukaryotic cellular processes. Proper function of the MVB pathway requires reversible membrane association of the ESCRTs, a process catalyzed by Vps4 ATPase. Vta1 regulates the Vps4 activity, but its mechanism of action was poorly understood. We report the high-resolution crystal structures of the Did2- and Vps60-binding N-terminal domain and the Vps4-binding C-terminal domain of S. cerevisiae Vta1. The C-terminal domain also mediates Vta1 dimerization and both subunits are required for its function as a Vps4 regulator. Emerging from our analysis is a mechanism of regulation by Vta1 in which the C-terminal domain stabilizes the ATP-dependent double ring assembly of Vps4. In addition, the MIT motif-containing N-terminal domain, projected by a long disordered linker, allows contact between the Vps4 disassembly machinery and the accessory ESCRT-III proteins. This provides an additional level of regulation and coordination for ESCRT-III assembly and disassembly.

==About this Structure==

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==Reference==

Structural basis of ~~vta1~~ function in the multivesicular body sorting pathway., Xiao J, Xia H, Zhou J, Azmi IF, Davies BA, Katzmann DJ, Xu Z, Dev Cell. 2008 Jan;14(1):37-49. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18194651 18194651]

Structural basis of Vta1 function in the multivesicular body sorting pathway., Xiao J, Xia H, Zhou J, Azmi IF, Davies BA, Katzmann DJ, Xu Z, Dev Cell. 2008 Jan;14(1):37-49. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18194651 18194651]

[[Category: Saccharomyces cerevisiae]]

[[Category: Single protein]]

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[[Category: transport]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The MVB pathway plays essential roles in several eukaryotic cellular, processes. Proper function of the MVB pathway requires reversible membrane, association of the ESCRTs, a process catalyzed by Vps4 ATPase. Vta1, regulates the Vps4 activity, but its mechanism of action was poorly, understood. We report the high-resolution crystal structures of the Did2-, and Vps60-binding N-terminal domain and the Vps4-binding C-terminal domain, of S. cerevisiae Vta1. The C-terminal domain also mediates Vta1, dimerization and both subunits are required for its function as a Vps4, regulator. Emerging from our analysis is a mechanism of regulation by Vta1, in which the C-terminal domain stabilizes the ATP-dependent double ring, assembly of Vps4. In addition, the MIT motif-containing N-terminal domain, projected by a long disordered linker, allows contact between the Vps4, disassembly machinery and the accessory ESCRT-III proteins. This provides, an additional level of regulation and coordination for ESCRT-III assembly, and disassembly.
+The MVB pathway plays essential roles in several eukaryotic cellular processes. Proper function of the MVB pathway requires reversible membrane association of the ESCRTs, a process catalyzed by Vps4 ATPase. Vta1 regulates the Vps4 activity, but its mechanism of action was poorly understood. We report the high-resolution crystal structures of the Did2- and Vps60-binding N-terminal domain and the Vps4-binding C-terminal domain of S. cerevisiae Vta1. The C-terminal domain also mediates Vta1 dimerization and both subunits are required for its function as a Vps4 regulator. Emerging from our analysis is a mechanism of regulation by Vta1 in which the C-terminal domain stabilizes the ATP-dependent double ring assembly of Vps4. In addition, the MIT motif-containing N-terminal domain, projected by a long disordered linker, allows contact between the Vps4 disassembly machinery and the accessory ESCRT-III proteins. This provides an additional level of regulation and coordination for ESCRT-III assembly and disassembly.
 ==About this Structure==
@@ Line 10: / Line 10: @@
 ==Reference==
-Structural basis of vta1 function in the multivesicular body sorting pathway., Xiao J, Xia H, Zhou J, Azmi IF, Davies BA, Katzmann DJ, Xu Z, Dev Cell. 2008 Jan;14(1):37-49. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18194651 18194651]
+Structural basis of Vta1 function in the multivesicular body sorting pathway., Xiao J, Xia H, Zhou J, Azmi IF, Davies BA, Katzmann DJ, Xu Z, Dev Cell. 2008 Jan;14(1):37-49. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18194651 18194651]
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
@@ Line 25: / Line 25: @@
 [[Category: transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 10:55:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:48:05 2008''