Issue 27, 2012

Incorporation of a fluorous diazirine group into phosphatidylinositol 4,5-bisphosphate to illustrate its interaction with ADP-ribosylation factor 1

Abstract

Phosphatidylinositides are one family of the most versatile signaling molecules in cells, yet how they interact with different proteins to regulate biological processes is not well understood. Towards a general strategy to identify phosphatidylinositide–protein interactions, a fluorous diazirine group has been incorporated into phosphatidylinositol 4,5-bisphosphate (PIP2). The modified PIP2 was effectively cleaved by phospholipase C, one signaling protein that utilizes PIP2 as its endogenous substrate. Upon light illumination, the PIP2 probe effectively crosslinks with small GTPase ADP-ribosylation 1 to form a complex, suggesting that the probe might be suitable to identify PIP2-interacting proteins on the proteome level.

Graphical abstract: Incorporation of a fluorous diazirine group into phosphatidylinositol 4,5-bisphosphate to illustrate its interaction with ADP-ribosylation factor 1

Supplementary files

Article information

Article type
Communication
Submitted
06 Feb 2012
Accepted
01 Jun 2012
First published
01 Jun 2012

Org. Biomol. Chem., 2012,10, 5197-5201

Incorporation of a fluorous diazirine group into phosphatidylinositol 4,5-bisphosphate to illustrate its interaction with ADP-ribosylation factor 1

W. Huang, W. Sun, Z. Song, Y. Yu, X. Chen and Q. Zhang, Org. Biomol. Chem., 2012, 10, 5197 DOI: 10.1039/C2OB25276G

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