English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Control of the terminal step of intracellular membrane fusion by protein phosphatase 1

MPS-Authors
/persons/resource/persons275906

Peters,  C
Mayer Group, Friedrich Miescher Laboratory, Max Planck Society;

/persons/resource/persons277039

Cesaro-Tadic,  S
Mayer Group, Friedrich Miescher Laboratory, Max Planck Society;

/persons/resource/persons277035

Glatz,  A
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 (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Peters, C., Andrews, P., Stark, M., Cesaro-Tadic, S., Glatz, A., Podtelejnikov, A., et al. (1999). Control of the terminal step of intracellular membrane fusion by protein phosphatase 1. Science, 285(5430), 1084-1087. doi:10.1126/science.285.5430.1084.


Cite as: https://hdl.handle.net/21.11116/0000-000A-DCEA-7
Abstract
Intracellular membrane fusion is crucial for the biogenesis and maintenance of cellular compartments, for vesicular traffic between them, and for exo- and endocytosis. Parts of the molecular machinery underlying this process have been identified, but most of these components operate in mutual recognition of the membranes. Here it is shown that protein phosphatase 1 (PP1) is essential for bilayer mixing, the last step of membrane fusion. PP1 was also identified in a complex that contained calmodulin, the second known factor implicated in the regulation of bilayer mixing. The PP1-calmodulin complex was required at multiple sites of intracellular trafficking; hence, PP1 may be a general factor controlling membrane bilayer mixing.