betaIV spectrin is recruited to axon initial segments and nodes of Ranvier by ankyrinG. Export

@article{citeulike:1692989, abstract = {High densities of ion channels at axon initial segments (AISs) and nodes of Ranvier are required for initiation, propagation, and modulation of action potentials in axons. The organization of these membrane domains depends on a specialized cytoskeleton consisting of two submembranous cytoskeletal and scaffolding proteins, ankyrinG (ankG) and betaIV spectrin. However, it is not known which of these proteins is the principal organizer, or if the mechanisms governing formation of the cytoskeleton at the AIS also apply to nodes. We identify a distinct protein domain in betaIV spectrin required for its localization to the AIS, and show that this domain mediates betaIV spectrin's interaction with ankG. Dominant-negative ankG disrupts betaIV spectrin localization, but does not alter endogenous ankG or Na(+) channel clustering at the AIS. Finally, using adenovirus for transgene delivery into myelinated neurons, we demonstrate that betaIV spectrin recruitment to nodes of Ranvier also depends on binding to ankG.}, address = {Department of Neuroscience, University of Connecticut Health Center, University of Connecticut, Farmington, CT 06032, USA.}, author = {Yang, Y. and Ogawa, Y. and Hedstrom, K. L. and Rasband, M. N.}, citeulike-article-id = {1692989}, citeulike-linkout-0 = {http://dx.doi.org/10.1083/jcb.200610128}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/17283186}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=17283186}, doi = {10.1083/jcb.200610128}, issn = {0021-9525}, journal = {J Cell Biol}, month = {February}, number = {4}, pages = {509--519}, posted-at = {2007-09-25 14:36:01}, priority = {0}, title = {betaIV spectrin is recruited to axon initial segments and nodes of Ranvier by ankyrinG.}, url = {http://dx.doi.org/10.1083/jcb.200610128}, volume = {176}, year = {2007} }

TY - JOUR ID - citeulike:1692989 L3 - citeulike-article-id:1692989 N2 - High densities of ion channels at axon initial segments (AISs) and nodes of Ranvier are required for initiation, propagation, and modulation of action potentials in axons. The organization of these membrane domains depends on a specialized cytoskeleton consisting of two submembranous cytoskeletal and scaffolding proteins, ankyrinG (ankG) and betaIV spectrin. However, it is not known which of these proteins is the principal organizer, or if the mechanisms governing formation of the cytoskeleton at the AIS also apply to nodes. We identify a distinct protein domain in betaIV spectrin required for its localization to the AIS, and show that this domain mediates betaIV spectrin's interaction with ankG. Dominant-negative ankG disrupts betaIV spectrin localization, but does not alter endogenous ankG or Na(+) channel clustering at the AIS. Finally, using adenovirus for transgene delivery into myelinated neurons, we demonstrate that betaIV spectrin recruitment to nodes of Ranvier also depends on binding to ankG. IS - 4 JF - J Cell Biol SN - 0021-9525 AD - Department of Neuroscience, University of Connecticut Health Center, University of Connecticut, Farmington, CT 06032, USA. EP - 519 TI - betaIV spectrin is recruited to axon initial segments and nodes of Ranvier by ankyrinG. VL - 176 SP - 509 AU - Yang, Y AU - Ogawa, Y AU - Hedstrom, KL AU - Rasband, MN PY - 2007/02/12/ UR - http://dx.doi.org/10.1083/jcb.200610128 ER -