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Gene Review

unc-64  -  Protein UNC-64

Caenorhabditis elegans

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Disease relevance of Syntaxin


Psychiatry related information on Syntaxin

  • Mutants were isolated by their ability to suppress lethargy of an unc-64 syntaxin mutant that restricts neurotransmitter release [2].

High impact information on Syntaxin

  • The syntaxin allelic variation was striking, particularly for isoflurane, where a 33-fold range of sensitivities was seen [1].
  • By screening existing mutants of the nematode Caenorhabditis elegans, we found that a mutation in the neuronal syntaxin gene dominantly conferred resistance to the VAs isoflurane and halothane [1].
  • Work in the past year has revealed that Unc-13 and Rab3a-interacting molecule regulate the conformational state of syntaxin to prime synaptic vesicle fusion [3].
  • Recent evidence that a syntaxin is required for cytokinesis in Caenorhabditis elegans embryos suggests that the mechanism of cell division in plant and animal cells may be more similar than previously imagined [4].
  • Here we describe the cloning, and the molecular and genetic characterization of the unc-64 gene, especially in relation to unc-18. unc-64 encodes a protein (C. elegans syntaxin) showing sequence and structural similarities to mammalian syntaxin 1A [5].

Biological context of Syntaxin

  • The PKC-catalyzed phosphorylation of Munc-18 inhibits its interaction with syntaxin [6].
  • However, nematode syntaxin appears not to be required for embryonic development, for secretion of cuticle from the hypodermis, or for the function of muscle, in contrast to Drosophila syntaxin, which appears to be required in all cells [7].
  • Caenorhabditis elegans TOM-1 is orthologous to vertebrate tomosyn, a cytosolic syntaxin-binding protein implicated in the modulation of both constitutive and regulated exocytosis [8].

Anatomical context of Syntaxin


Associations of Syntaxin with chemical compounds

  • As assessed by pharmacological criteria, halothane and isoflurane themselves reduced cholinergic transmission, and the presynaptic anesthetic effect was blocked by the resistant syntaxin mutation [1].
  • Furthermore, rabphilin mutations display strong synergistic interactions with hypomorphic lesions in the syntaxin, synaptosomal-associated protein of 25 kDa, and synaptobrevin soluble N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) genes; double mutants were nonresponsive to mechanical stimulation [9].


  1. A neomorphic syntaxin mutation blocks volatile-anesthetic action in Caenorhabditis elegans. van Swinderen, B., Saifee, O., Shebester, L., Roberson, R., Nonet, M.L., Crowder, C.M. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  2. SLO-1 potassium channels control quantal content of neurotransmitter release at the C. elegans neuromuscular junction. Wang, Z.W., Saifee, O., Nonet, M.L., Salkoff, L. Neuron (2001) [Pubmed]
  3. The synaptic vesicle cycle: exocytosis and endocytosis in Drosophila and C. elegans. Richmond, J.E., Broadie, K.S. Curr. Opin. Neurobiol. (2002) [Pubmed]
  4. Cell division: plant-like properties of animal cell cytokinesis. Bowerman, B., Severson, A.F. Curr. Biol. (1999) [Pubmed]
  5. Functional properties of the unc-64 gene encoding a Caenorhabditis elegans syntaxin. Ogawa, H., Harada, S., Sassa, T., Yamamoto, H., Hosono, R. J. Biol. Chem. (1998) [Pubmed]
  6. Phosphorylation of Munc-18/n-Sec1/rbSec1 by protein kinase C: its implication in regulating the interaction of Munc-18/n-Sec1/rbSec1 with syntaxin. Fujita, Y., Sasaki, T., Fukui, K., Kotani, H., Kimura, T., Hata, Y., Südhof, T.C., Scheller, R.H., Takai, Y. J. Biol. Chem. (1996) [Pubmed]
  7. The Caenorhabditis elegans unc-64 locus encodes a syntaxin that interacts genetically with synaptobrevin. Saifee, O., Wei, L., Nonet, M.L. Mol. Biol. Cell (1998) [Pubmed]
  8. Tomosyn Inhibits Synaptic Vesicle Priming in Caenorhabditis elegans. Gracheva, E.O., Burdina, A.O., Holgado, A.M., Berthelot-Grosjean, M., Ackley, B.D., Hadwiger, G., Nonet, M.L., Weimer, R.M., Richmond, J.E. PLoS Biol. (2006) [Pubmed]
  9. Rabphilin potentiates soluble N-ethylmaleimide sensitive factor attachment protein receptor function independently of rab3. Staunton, J., Ganetzky, B., Nonet, M.L. J. Neurosci. (2001) [Pubmed]
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