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  Structural and functional characterization of the two phosphoinositide binding sites of PROPPINs.

Krick, R., Busse, R. A., Scacioc, A., Stephan, M., Janshoff, A., Thumm, M., et al. (2012). Structural and functional characterization of the two phosphoinositide binding sites of PROPPINs. Proceedings of the National Academy of Sciences of the United States of America, 109(30), E2042-E2049. doi:10.1073/pnas.1205128109.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000F-A21F-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-80DC-4
Genre: Journal Article

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 Creators:
Krick, R., Author
Busse, R. A.1, Author              
Scacioc, A.1, Author              
Stephan, M., Author
Janshoff, A., Author
Thumm, M., Author
Kühnel, K.1, Author              
Affiliations:
1Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              

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Free keywords: Autophagy; protein-lipid interactions; X-ray crystallography; yeast
 Abstract: β-propellers that bind polyphosphoinositides (PROPPINs), a eukaryotic WD-40 motif-containing protein family, bind via their predicted β-propeller fold the polyphosphoinositides PtdIns3P and PtdIns(3,5)P2 using a conserved FRRG motif. PROPPINs play a key role in macroautophagy in addition to other functions. We present the 3.0-Å crystal structure of Kluyveromyces lactis Hsv2, which shares significant sequence homologies with its three Saccharomyces cerevisiae homologs Atg18, Atg21, and Hsv2. It adopts a seven-bladed β-propeller fold with a rare nonvelcro propeller closure. Remarkably, in the crystal structure, the two arginines of the FRRG motif are part of two distinct basic pockets formed by a set of highly conserved residues. In comprehensive in vivo and in vitro studies of ScAtg18 and ScHsv2, we define within the two pockets a set of conserved residues essential for normal membrane association, phosphoinositide binding, and biological activities. Our experiments show that PROPPINs contain two individual phosphoinositide binding sites. Based on docking studies, we propose a model for phosphoinositide binding of PROPPINs.

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Language(s): eng - English
 Dates: 2012-07-022012-07-24
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1073/pnas.1205128109
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Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
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Pages: - Volume / Issue: 109 (30) Sequence Number: - Start / End Page: E2042 - E2049 Identifier: -