It takes two to tango: PROPPINs use two phosphoinositide-binding sites.

Thumm, M.; Busse, R. A.; Scacioc, A.; Stephan, M.; Janshoff, A.; Kühnel, K.; Krick, R.

doi:10.4161/auto.22400

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

It takes two to tango: PROPPINs use two phosphoinositide-binding sites.

MPS-Authors

/persons/resource/persons71883

Busse, R. A.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons71881

Scacioc, A.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15388

Kühnel, K.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

External Resource

https://www.landesbioscience.com/journals/autophagy/2012AUTO0430R.pdf
(Publisher version)

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

Thumm, M., Busse, R. A., Scacioc, A., Stephan, M., Janshoff, A., Kühnel, K., et al. (2013). It takes two to tango: PROPPINs use two phosphoinositide-binding sites. Autophagy, 9(1), 106-107. doi:10.4161/auto.22400.

Cite as: https://hdl.handle.net/11858/00-001M-0000-000E-DDEE-4

Abstract

PROPPINs are a family of PtdIns3P and PtdIns(3,5)P2-binding proteins. The crystal structure now unravels the presence of two distinct phosphoinositide-binding sites at the circumference of the seven bladed β-propeller. Mutagenesis analysis of the binding sites shows that both are required for normal membrane association and autophagic activities. We identified a set of evolutionarily conserved basic and polar residues within both binding pockets, which are crucial for phosphoinositide binding. We expect that membrane association of PROPPINs is further stabilized by membrane insertions and interactions with other proteins