Primordial neurosecretory apparatus identified in the choanoflagellate Monosiga brevicollis
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Primordial neurosecretory apparatus identified in the choanoflagellate Monosiga brevicollis. / Burkhardt, Pawel; Stegmann, Christian M; Cooper, Benjamin; Kloepper, Tobias H; Imig, Cordelia; Varoqueaux, Frédérique; Wahl, Markus C; Fasshauer, Dirk.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 108, No. 37, 13.09.2011, p. 15264-9.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Primordial neurosecretory apparatus identified in the choanoflagellate Monosiga brevicollis
AU - Burkhardt, Pawel
AU - Stegmann, Christian M
AU - Cooper, Benjamin
AU - Kloepper, Tobias H
AU - Imig, Cordelia
AU - Varoqueaux, Frédérique
AU - Wahl, Markus C
AU - Fasshauer, Dirk
PY - 2011/9/13
Y1 - 2011/9/13
N2 - SNARE protein-driven secretion of neurotransmitters from synaptic vesicles is at the center of neuronal communication. In the absence of the cytosolic protein Munc18-1, synaptic secretion comes to a halt. Although it is believed that Munc18-1 orchestrates SNARE complexes, its mode of action is still a matter of debate. In particular, it has been challenging to clarify the role of a tight Munc18/syntaxin 1 complex, because this interaction interferes strongly with syntaxin's ability to form a SNARE complex. In this complex, two regions of syntaxin, the N-peptide and the remainder in closed conformation, bind to Munc18 simultaneously. Until now, this binary complex has been reported for neuronal tissues only, leading to the hypothesis that it might be a specialization of the neuronal secretion apparatus. Here we aimed, by comparing the core secretion machinery of the unicellular choanoflagellate Monosiga brevicollis with that of animals, to reconstruct the ancestral function of the Munc18/syntaxin1 complex. We found that the Munc18/syntaxin 1 complex from M. brevicollis is structurally and functionally highly similar to the vertebrate complex, suggesting that it constitutes a fundamental step in the reaction pathway toward SNARE assembly. We thus propose that the primordial secretion machinery of the common ancestor of choanoflagellates and animals has been co-opted for synaptic roles during the rise of animals.
AB - SNARE protein-driven secretion of neurotransmitters from synaptic vesicles is at the center of neuronal communication. In the absence of the cytosolic protein Munc18-1, synaptic secretion comes to a halt. Although it is believed that Munc18-1 orchestrates SNARE complexes, its mode of action is still a matter of debate. In particular, it has been challenging to clarify the role of a tight Munc18/syntaxin 1 complex, because this interaction interferes strongly with syntaxin's ability to form a SNARE complex. In this complex, two regions of syntaxin, the N-peptide and the remainder in closed conformation, bind to Munc18 simultaneously. Until now, this binary complex has been reported for neuronal tissues only, leading to the hypothesis that it might be a specialization of the neuronal secretion apparatus. Here we aimed, by comparing the core secretion machinery of the unicellular choanoflagellate Monosiga brevicollis with that of animals, to reconstruct the ancestral function of the Munc18/syntaxin1 complex. We found that the Munc18/syntaxin 1 complex from M. brevicollis is structurally and functionally highly similar to the vertebrate complex, suggesting that it constitutes a fundamental step in the reaction pathway toward SNARE assembly. We thus propose that the primordial secretion machinery of the common ancestor of choanoflagellates and animals has been co-opted for synaptic roles during the rise of animals.
KW - Choanoflagellata/cytology
KW - Crystallography, X-Ray
KW - Detergents/pharmacology
KW - Munc18 Proteins/chemistry
KW - Neurosecretory Systems/drug effects
KW - Phylogeny
KW - Protein Binding/drug effects
KW - Protein Structure, Secondary
KW - SNARE Proteins/metabolism
KW - Synapses/drug effects
KW - Syntaxin 1/chemistry
KW - Thermodynamics
U2 - 10.1073/pnas.1106189108
DO - 10.1073/pnas.1106189108
M3 - Journal article
C2 - 21876177
VL - 108
SP - 15264
EP - 15269
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 37
ER -
ID: 237698285