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Discovery of LRE1 as a specific and allosteric inhibitor of soluble adenylyl cyclase

Title data

Ramos-Espiritu, Lavoisier ; Kleinbölting, Silke ; Navarrete, Felipe A. ; Alvau, Antonio ; Visconti, Pablo E. ; Valsecchi, Federica ; Starkov, Anatoly ; Manfredi, Giovanni ; Buck, Hannes ; Adura, Carolina ; Zippin, Jonathan H. ; van den Heuvel, Joop ; Glickman, J. Fraser ; Steegborn, Clemens ; Levin, Lonny R. ; Buck, Jochen:
Discovery of LRE1 as a specific and allosteric inhibitor of soluble adenylyl cyclase.
In: Nature Chemical Biology. Vol. 12 (October 2016) Issue 10 . - pp. 838-844.
ISSN 1552-4469
DOI: https://doi.org/10.1038/nchembio.2151

Abstract in another language

The prototypical second messenger cAMP regulates a wide variety of physiological processes. It can simultaneously mediate diverse functions by acting locally in independently regulated microdomains. In mammalian cells, two types of adenylyl cyclase generate cAMP: G-protein-regulated transmembrane adenylyl cyclases and bicarbonate-, calcium- and ATP-regulated soluble adenylyl cyclase (sAC). Because each type of cyclase regulates distinct microdomains, methods to distinguish between them are needed to understand cAMP signaling. We developed a mass-spectrometry-based adenylyl cyclase assay, which we used to identify a new sAC-specific inhibitor, LRE1. LRE1 bound to the bicarbonate activator binding site and inhibited sAC via a unique allosteric mechanism. LRE1 prevented sAC-dependent processes in cellular and physiological systems, and it will facilitate exploration of the therapeutic potential of sAC inhibition.

Further data

Item Type: Article in a journal
Refereed: No
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Clemens Steegborn
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: No
DDC Subjects: 500 Science
500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 06 Apr 2017 08:57
Last Modified: 26 Nov 2018 08:14
URI: https://eref.uni-bayreuth.de/id/eprint/36767