TY - JOUR
T1 - GluR1 controls dendrite growth through its binding partner, SAP97
AU - Zhou, Weiguo
AU - Zhang, Lei
AU - Guoxiang, Xiong
AU - Mojsilovic-Petrovic, Jelena
AU - Takamaya, Kogo
AU - Sattler, Rita
AU - Huganir, Richard
AU - Kalb, Robert
PY - 2008/10/8
Y1 - 2008/10/8
N2 - Activity-dependent dendrite elaboration influences the pattern of interneuronal connectivity and network function. In the present study, we examined the mechanism by which the GluR1 subunit of AMPA receptors controls dendrite morphogenesis. GluR1 binds to SAP97, a scaffolding protein that is a component of the postsynaptic density, via its C-terminal 7 aa. We find that elimination of this interaction in vitro or in vivo (by deleting the C-terminal 7 aa of GluR1, GluR1Δ7) does not influence trafficking, processing, or cell surface GluR1 expression but does prevent translocation of SAP97 from the cytosol to membranes. GluR1 and SAP97 together at the plasma membrane promotes dendrite branching in an activity-dependent manner, although this does not require physical association. Our findings suggest that the C-terminal 7 aa of GluR1 are essential for bringing SAP97 to the plasma membrane, where it acts to translate the activity of AMPA receptors into dendrite growth.
AB - Activity-dependent dendrite elaboration influences the pattern of interneuronal connectivity and network function. In the present study, we examined the mechanism by which the GluR1 subunit of AMPA receptors controls dendrite morphogenesis. GluR1 binds to SAP97, a scaffolding protein that is a component of the postsynaptic density, via its C-terminal 7 aa. We find that elimination of this interaction in vitro or in vivo (by deleting the C-terminal 7 aa of GluR1, GluR1Δ7) does not influence trafficking, processing, or cell surface GluR1 expression but does prevent translocation of SAP97 from the cytosol to membranes. GluR1 and SAP97 together at the plasma membrane promotes dendrite branching in an activity-dependent manner, although this does not require physical association. Our findings suggest that the C-terminal 7 aa of GluR1 are essential for bringing SAP97 to the plasma membrane, where it acts to translate the activity of AMPA receptors into dendrite growth.
KW - Motor neurons
KW - Postsynaptic density
KW - Scaffold protein
KW - Spinal cord
KW - Synaptic activity
KW - Trafficking
UR - http://www.scopus.com/inward/record.url?scp=55249105043&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=55249105043&partnerID=8YFLogxK
U2 - 10.1523/JNEUROSCI.3434-08.2008
DO - 10.1523/JNEUROSCI.3434-08.2008
M3 - Article
C2 - 18842882
AN - SCOPUS:55249105043
SN - 0270-6474
VL - 28
SP - 10220
EP - 10233
JO - Journal of Neuroscience
JF - Journal of Neuroscience
IS - 41
ER -