English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Role of the Vtc proteins in V-ATPase stability and membrane trafficking

MPS-Authors
/persons/resource/persons275910

Müller,  O
Mayer Group, Friedrich Miescher Laboratory, Max Planck Society;

/persons/resource/persons275913

Neumann,  H
Mayer Group, Friedrich Miescher Laboratory, Max Planck Society;

/persons/resource/persons275899

Bayer,  MJ
Mayer Group, Friedrich Miescher Laboratory, Max Planck Society;

/persons/resource/persons275880

Mayer,  A
Mayer Group, Friedrich Miescher Laboratory, Max Planck Society;

External Resource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Müller, O., Neumann, H., Bayer, M., & Mayer, A. (2003). Role of the Vtc proteins in V-ATPase stability and membrane trafficking. Journal of Cell Science, 116(6), 1107-1115. doi:10.1242/jcs.00328.


Cite as: http://hdl.handle.net/21.11116/0000-000A-B16B-6
Abstract
Vtc proteins have genetic and physical relations with the vacuolar H(+)-ATPase (V-ATPase), influence vacuolar H(+) uptake and, like the V-ATPase V(0) sectors, are important factors in vacuolar membrane fusion. Vacuoles from vtc1delta and vtc4delta mutants had slightly reduced H(+)-uptake activity. These defects could be separated from Vtc function in vacuole fusion, demonstrating that Vtc proteins have a direct role in membrane fusion. We analyzed their involvement in other membrane trafficking steps and in VATPase dynamics. Deletion of VTC genes did not impede endocytic trafficking to the vacuole. However, ER to Golgi trafficking and further transport to the vacuole was delayed in deltavtc3 cells. In accordance with that, deltavtc3 cells showed a reduced growth rate. Vtc mutations did not interfere with regulated assembly and disassembly of the V-ATPase, but they affected the number of peripheral V(1) subunits associated with the vacuoles. deltavtc3 vacuoles carried significantly more V(1) subunits, whereas deltavtc1, deltavtc2 and deltavtc4 had significantly less. The proteolytic sensitivity of the V(0) subunit Vph1p was different in deltavtc and wild-type cells in vivo, corroborating the physical interaction of Vtc proteins with the V-ATPase observed in vitro. We suggest that Vtc proteins affect the conformation of V(0). They might thereby influence the stability of the VATPase holoenzyme and support the function of its V(0) sector in vacuolar membrane fusion.