Abstract:
: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.
journal_name
Sci Signaljournal_title
Science signalingauthors
Ioannou MS,Marat ALdoi
10.1126/scisignal.2002989subject
Has Abstractpub_date
2012-04-24 00:00:00pages
jc1issue
221eissn
1945-0877issn
1937-9145pii
scisignal.2002989journal_volume
5pub_type
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