cAMP acts on exchange protein activated by cAMP/cAMP-regulated guanine nucleotide exchange protein to regulate transmitter release at the crayfish neuromuscular junction.

@article{citeulike:303318, abstract = {Glutamatergic synapses are highly modifiable, suiting them for key roles in processes such as learning and memory. At crayfish glutamatergic neuromuscular junctions, hyperpolarization and cyclic nucleotide-activated (HCN) ion channels mediate hormonal modulation of glutamatergic synapses and a form activity-dependent long-term facilitation (LTF) of synaptic transmission. Here, we show that a new target for cAMP, exchange protein activated by cAMP (Epac) or cAMP-regulated guanine nucleotide exchange protein, is involved in the hormonal enhancement of synaptic transmission by serotonin. Induction of LTF "tags" synapses, rendering them responsive to cAMP in an HCN-independent manner. Epac also mediates the enhancement of tagged synapses. Thus, the cAMP-dependent enhancement of transmission is mediated by two separate pathways, neither of which involves protein kinase A.}, address = {Department of Molecular and Cell Biology and Helen Wills Neuroscience Institute, University of California, Berkeley, California 9472, USA.}, author = {Zhong, N. and Zucker, R. S. }, citeulike-article-id = {303318}, doi = {http://dx.doi.org/10.1523/JNEUROSCI.3703-04.2005}, issn = {1529-2401}, journal = {J Neurosci}, keywords = {camp, epac, hcn, lamotrigine, nmj}, month = {January}, number = {1}, pages = {208--214}, posted-at = {2005-08-25 11:43:11}, priority = {2}, title = {cAMP acts on exchange protein activated by cAMP/cAMP-regulated guanine nucleotide exchange protein to regulate transmitter release at the crayfish neuromuscular junction.}, url = {http://dx.doi.org/10.1523/JNEUROSCI.3703-04.2005}, volume = {25}, year = {2005} }

TY - JOUR ID - citeulike:303318 L3 - citeulike-article-id:303318 TI - cAMP acts on exchange protein activated by cAMP/cAMP-regulated guanine nucleotide exchange protein to regulate transmitter release at the crayfish neuromuscular junction. JF - J Neurosci VL - 25 IS - 1 SP - 208 EP - 214 AD - Department of Molecular and Cell Biology and Helen Wills Neuroscience Institute, University of California, Berkeley, California 9472, USA. SN - 1529-2401 N2 - Glutamatergic synapses are highly modifiable, suiting them for key roles in processes such as learning and memory. At crayfish glutamatergic neuromuscular junctions, hyperpolarization and cyclic nucleotide-activated (HCN) ion channels mediate hormonal modulation of glutamatergic synapses and a form activity-dependent long-term facilitation (LTF) of synaptic transmission. Here, we show that a new target for cAMP, exchange protein activated by cAMP (Epac) or cAMP-regulated guanine nucleotide exchange protein, is involved in the hormonal enhancement of synaptic transmission by serotonin. Induction of LTF "tags" synapses, rendering them responsive to cAMP in an HCN-independent manner. Epac also mediates the enhancement of tagged synapses. Thus, the cAMP-dependent enhancement of transmission is mediated by two separate pathways, neither of which involves protein kinase A. KW - camp KW - epac KW - hcn KW - lamotrigine KW - nmj AU - Zhong, N AU - Zucker, RS PY - 2005/01/05/ UR - http://dx.doi.org/10.1523/JNEUROSCI.3703-04.2005 ER -