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A Photo-clickable ATP-Mimetic Reveals Nucleotide Interactors in the Membrane Proteome.

Abstract：

:ATP is an important energy metabolite and allosteric signal in health and disease. ATP-interacting proteins, such as P2 receptors, control inflammation, cell death, migration, and wound healing. However, identification of allosteric ATP sites remains challenging, and our current inventory of ATP-controlled pathways is likely incomplete. Here, we develop and verify mipATP as a minimally invasive photoaffinity probe for ATP-interacting proteins. Its N6 functionalization allows target enrichment by UV crosslinking and conjugation to reporter tags by "click" chemistry. The additions are compact, allowing mipATP to completely retain the calcium signaling responses of native ATP in vitro and in vivo. mipATP specifically enriched for known nucleotide binders in A549 cell lysates and membrane fractions. In addition, it retrieved unannotated ATP interactors, such as the FAS receptor, CD44, and various SLC transporters. Thus, mipATP is a promising tool to identify allosteric ATP sites in the proteome.

journal_name

Cell Chem Biol

journal_title

Cell chemical biology

authors

Jelcic M,Wang K,Hui KL,Cai XC,Enyedi B,Luo M,Niethammer P

doi

10.1016/j.chembiol.2020.05.010

subject

Has Abstract

pub_date

2020-08-20 00:00:00

pages

1073-1083.e12

issue

8

eissn

2451-9456

issn

2451-9448

pii

S2451-9456(20)30187-2

journal_volume

27

pub_type

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