Key protein responsible for controlling communication between brain cells identified

You will have to ask someone else to tell how to put this into a stroke protocol. A great stroke association would do it if we had one.
A writeup on it here:
http://phys.org/news/2013-11-key-protein-responsible-brain-cells.html
The abstract here:
http://www.nature.com/emboj/journal/v32/n11/full/emboj201365a.html

Chun Guo¹, Keri L Hildick¹, Jia Luo¹, Laura Dearden¹, Kevin A Wilkinson¹ and Jeremy M Henley¹

1. School of Biochemistry, University of Bristol, University Walk, Bristol, UK

Correspondence to:

Jeremy M Henley, School of Biochemistry, University of Bristol, University Walk, Medical Sciences Building, Bristol BS8 1TD, UK. Tel.:+44 (0)117 331 1945; Fax:+44 (0)117 331 2168; E-mail: j.m.henley@bristol.ac.uk

Received 9 January 2013; Accepted 27 February 2013

Global increases in small ubiquitin-like modifier (SUMO)-2/3 conjugation are a neuroprotective response to severe stress but the mechanisms and specific target proteins that determine cell survival have not been identified. Here, we demonstrate that the SUMO-2/3-specific protease SENP3 is degraded during oxygen/glucose deprivation (OGD), an in vitro model of ischaemia, via a pathway involving the unfolded protein response (UPR) kinase PERK and the lysosomal enzyme cathepsin B. A key target for SENP3-mediated deSUMOylation is the GTPase Drp1, which plays a major role in regulating mitochondrial fission. We show that depletion of SENP3 prolongs Drp1 SUMOylation, which suppresses Drp1-mediated cytochrome c release and caspase-mediated cell death. SENP3 levels recover following reoxygenation after OGD allowing deSUMOylation of Drp1, which facilitates Drp1 localization at mitochondria and promotes fragmentation and cytochrome c release. RNAi knockdown of SENP3 protects cells from reoxygenation-induced cell death via a mechanism that requires Drp1 SUMOylation. Thus, we identify a novel adaptive pathway to extreme cell stress in which dynamic changes in SENP3 stability and regulation of Drp1 SUMOylation are crucial determinants of cell fate.