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EMBO Rep. 2015 Oct;16(10):1308-17. doi: 10.15252/embr.201540305. Epub 2015 Sep 3.

Evolutionary conservation of complexins: from choanoflagellates to mice.

Author information

1
Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute Stanford University School of Medicine, Stanford, CA, USA College of Biomedical Engineering, South-Central University for Nationalities, Wuhan, China sunlittlefly@hotmail.com tcs1@stanford.edu.
2
Department of Biophysics, Howard Hughes Medical Institute University of Texas Southwestern Medical Center, Dallas, TX, USA.
3
Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute Stanford University School of Medicine, Stanford, CA, USA.
4
Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute Stanford University School of Medicine, Stanford, CA, USA sunlittlefly@hotmail.com tcs1@stanford.edu.

Abstract

Complexins are synaptic SNARE complex-binding proteins that cooperate with synaptotagmins in activating Ca(2+)-stimulated, synaptotagmin-dependent synaptic vesicle exocytosis and in clamping spontaneous, synaptotagmin-independent synaptic vesicle exocytosis. Here, we show that complexin sequences are conserved in some non-metazoan unicellular organisms and in all metazoans, suggesting that complexins are a universal feature of metazoans that predate metazoan evolution. We show that complexin from Nematostella vectensis, a cnidarian sea anemone far separated from mammals in metazoan evolution, functionally replaces mouse complexins in activating Ca(2+)-triggered exocytosis, but is unable to clamp spontaneous exocytosis. Thus, the activating function of complexins is likely conserved throughout metazoan evolution.

KEYWORDS:

SNARE proteins; evolution; membrane fusion; synapse; synaptotagmin

PMID:
26338476
PMCID:
PMC4766454
DOI:
10.15252/embr.201540305
[Indexed for MEDLINE]
Free PMC Article

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