PT  - JOURNAL ARTICLE
AU  - Ioannou, Maria S.
AU  - Marat, Andrea L.
TI  - The Role of EHD Proteins at the Neuronal Synapse
AID  - 10.1126/scisignal.2002989
DP  - 2012 Apr 24
TA  - Science Signaling
PG  - jc1--jc1
VI  - 5
IP  - 221
4099  - http://stke.sciencemag.org/content/5/221/jc1.short
4100  - http://stke.sciencemag.org/content/5/221/jc1.full
SO  - Sci. Signal.2012 Apr 24; 5
AB  - Eps15 homology domain (EHD) proteins are conserved adenosine triphosphatases that are involved in membrane remodeling. EHD family members are structurally similar to the guanosine triphosphatase (GTPase) dynamin, and both are essential for the fission step of clathrin-mediated endocytosis. This Journal Club highlights a recent study by Jakobsson et al. that reports the unexpected finding that, rather than having a redundant function, EHD can regulate dynamin activity. Dynamin helices assemble around the neck of budding endocytic vesicles; as dynamin helices lengthen, the neck of the growing bud may become so long that GTP hydrolysis is no longer sufficient to promote fission. EHD increases the efficiency of dynamin-induced fission by restricting the length of dynamin helices. Furthermore, EHD is able to bind both dynamin and amphiphysin. Therefore, we propose a model whereby amphiphysin recruits both EHD and dynamin in neurons to regulate clathrin-dependent synaptic vesicle endocytosis.