PKC-induced intracellular trafficking of Ca(V)2 precedes its rapid recruitment to the plasma membrane. Export

@article{citeulike:3852113, abstract = {Activation of protein kinase C (PKC) potentiates secretion in Aplysia peptidergic neurons, in part by inducing new sites for peptide release at growth cone terminals. The mechanisms by which ion channels are trafficked to such sites are, however, not well understood. We now show that PKC activation rapidly recruits new Ca(V)2 subunits to the plasma membrane, and that recruitment is blocked by latrunculin B, an inhibitor of actin polymerization. In contrast, inhibition of microtubule polymerization selectively prevents the appearance of Ca(V)2 subunits only at the distal edge of the growth cone. In resting neurons, Ca(V)2-containing organelles reside in the central region of growth cones, but are absent from distal lamellipodia. After activation of PKC, these organelles are transported on microtubules to the lamellipodium. The ability to traffic to the most distal sites of channel insertion inside the lamellipodium does, therefore, not require intact actin but requires intact microtubules. Only after activation of PKC do Ca(V)2 channels associate with actin and undergo insertion into the plasma membrane.}, author = {Zhang, Y. and Helm, J. S. and Senatore, A. and Spafford, J. D. and Kaczmarek, L. K. and Jonas, E. A.}, citeulike-article-id = {3852113}, citeulike-linkout-0 = {http://dx.doi.org/10.1523/JNEUROSCI.4314-07}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/18322103}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=18322103}, comment = {extracellular antibody against S1-S2 of domain II}, doi = {10.1523/JNEUROSCI.4314-07}, issn = {1529-2401}, journal = {The Journal of neuroscience : the official journal of the Society for Neuroscience}, keywords = {aplysia, exocytosis, ion-channels, surface-expression, trafficking}, month = {March}, number = {10}, pages = {2601--2612}, posted-at = {2009-01-06 09:59:45}, priority = {0}, title = {PKC-induced intracellular trafficking of Ca(V)2 precedes its rapid recruitment to the plasma membrane.}, url = {http://dx.doi.org/10.1523/JNEUROSCI.4314-07}, volume = {28}, year = {2008} }

TY - JOUR ID - citeulike:3852113 L3 - citeulike-article-id:3852113 N2 - Activation of protein kinase C (PKC) potentiates secretion in Aplysia peptidergic neurons, in part by inducing new sites for peptide release at growth cone terminals. The mechanisms by which ion channels are trafficked to such sites are, however, not well understood. We now show that PKC activation rapidly recruits new Ca(V)2 subunits to the plasma membrane, and that recruitment is blocked by latrunculin B, an inhibitor of actin polymerization. In contrast, inhibition of microtubule polymerization selectively prevents the appearance of Ca(V)2 subunits only at the distal edge of the growth cone. In resting neurons, Ca(V)2-containing organelles reside in the central region of growth cones, but are absent from distal lamellipodia. After activation of PKC, these organelles are transported on microtubules to the lamellipodium. The ability to traffic to the most distal sites of channel insertion inside the lamellipodium does, therefore, not require intact actin but requires intact microtubules. Only after activation of PKC do Ca(V)2 channels associate with actin and undergo insertion into the plasma membrane. IS - 10 JF - The Journal of neuroscience : the official journal of the Society for Neuroscience SN - 1529-2401 EP - 2612 TI - PKC-induced intracellular trafficking of Ca(V)2 precedes its rapid recruitment to the plasma membrane. VL - 28 SP - 2601 KW - aplysia KW - exocytosis KW - ion-channels KW - surface-expression KW - trafficking N1 - extracellular antibody against S1-S2 of domain II AU - Zhang, Y AU - Helm, JS AU - Senatore, A AU - Spafford, JD AU - Kaczmarek, LK AU - Jonas, EA PY - 2008/03/05/ UR - http://dx.doi.org/10.1523/JNEUROSCI.4314-07 ER -