TY - JOUR
T1 - LL5β
T2 - A regulator of postsynaptic differentiation identified in a screen for synaptically enriched transcripts at the neuromuscular junction
AU - Kishi, Masashi
AU - Kummer, Terrance T.
AU - Eglen, Stephen J.
AU - Sanes, Joshua R.
PY - 2005/4/25
Y1 - 2005/4/25
N2 - In both neurons and muscle fibers, specific mRNAs are concentrated beneath and locally translated at synaptic sites. At the skeletal neuromuscular junction, all synaptic RNAs identified to date encode synaptic components. Using microarrays, we compared RNAs in synapse-rich and -free regions of muscles, thereby identifying transcripts that are enriched near synapses and that encode soluble membrane and nuclear proteins. One gene product, LL5β, binds to both phosphoinositides and a cytoskeletal protein, filamin, one form of which is concentrated at synaptic sites. LL5β is itself associated with the cytoplasmic face of the postsynaptic membrane; its highest levels border regions of highest acetylcholine receptor (AChR) density, which suggests a role in "corraling" AChRs. Consistent with this idea, perturbing LL5β expression in myotubes inhibits AChR aggregation. Thus, a strategy designed to identify novel synaptic components led to identification of a protein required for assembly of the postsynaptic apparatus.
AB - In both neurons and muscle fibers, specific mRNAs are concentrated beneath and locally translated at synaptic sites. At the skeletal neuromuscular junction, all synaptic RNAs identified to date encode synaptic components. Using microarrays, we compared RNAs in synapse-rich and -free regions of muscles, thereby identifying transcripts that are enriched near synapses and that encode soluble membrane and nuclear proteins. One gene product, LL5β, binds to both phosphoinositides and a cytoskeletal protein, filamin, one form of which is concentrated at synaptic sites. LL5β is itself associated with the cytoplasmic face of the postsynaptic membrane; its highest levels border regions of highest acetylcholine receptor (AChR) density, which suggests a role in "corraling" AChRs. Consistent with this idea, perturbing LL5β expression in myotubes inhibits AChR aggregation. Thus, a strategy designed to identify novel synaptic components led to identification of a protein required for assembly of the postsynaptic apparatus.
UR - http://www.scopus.com/inward/record.url?scp=18544369905&partnerID=8YFLogxK
U2 - 10.1083/jcb.200411012
DO - 10.1083/jcb.200411012
M3 - Article
C2 - 15851520
AN - SCOPUS:18544369905
SN - 0021-9525
VL - 169
SP - 355
EP - 366
JO - Journal of Cell Biology
JF - Journal of Cell Biology
IS - 2
ER -