TY  - JOUR
AU  - Mastny, Markus
AU  - Heuck, Alexander
AU  - Kurzbauer, Robert
AU  - Heiduk, Anja
AU  - Boisguerin, Prisca
AU  - Volkmer, Rudolf
AU  - Ehrmann, Michael
AU  - Rodrigues, Christopher D. A.
AU  - Rudner, David Z.
AU  - Clausen, Tim
TI  - CtpB Assembles a Gated Protease Tunnel Regulating Cell-Cell Signaling during Spore Formation in Bacillus subtilis
JO  - Cell
VL  - 155
IS  - 3
SN  - 0092-8674
CY  - [Cambridge, Mass.]
PB  - Cell Press
M1  - DESY-2014-02420
SP  - 647 - 658
PY  - 2013
N1  - (c) Elsevier Inc.
AB  - Spore formation in Bacillus subtilis relies on a regulated intramembrane proteolysis (RIP) pathway that synchronizes mother-cell and forespore development. To address the molecular basis of this SpoIV transmembrane signaling, we carried out a structure-function analysis of the activating protease CtpB. Crystal structures reflecting distinct functional states show that CtpB constitutes a ring-like protein scaffold penetrated by two narrow tunnels. Access to the proteolytic sites sequestered within these tunnels is controlled by PDZ domains that rearrange upon substrate binding. Accordingly, CtpB resembles a minimal version of a self-compartmentalizing protease regulated by a unique allosteric mechanism. Moreover, biochemical analysis of the PDZ-gated channel combined with sporulation assays reveal that activation of the SpoIV RIP pathway is induced by the concerted activity of CtpB and a second signaling protease, SpoIVB. This proteolytic mechanism is of broad relevance for cell-cell communication, illustrating how distinct signaling pathways can be integrated into a single RIP module.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000326571800018
C6  - pmid:24243021
DO  - DOI:10.1016/j.cell.2013.09.050
UR  - https://bib-pubdb1.desy.de/record/168215
ER  -