Structure-function analysis of SAP97, a modular scaffolding protein that drives dendrite growth

L. Zhang; F. C. Hsu; J. Mojsilovic-Petrovic; A. M. Jablonski; J. Zhai; D. A. Coulter; R. G. Kalb

doi:10.1016/j.mcn.2015.02.011

Structure-function analysis of SAP97, a modular scaffolding protein that drives dendrite growth

L. Zhang, F. C. Hsu, J. Mojsilovic-Petrovic, A. M. Jablonski, J. Zhai, D. A. Coulter, R. G. Kalb^*

^*Corresponding author for this work

Neurology

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

Abstract

Activation of AMPA receptors assembled with the GluA1 subunit can promote dendrite growth in a manner that depends on its direct binding partner, SAP97. SAP97 is a modular scaffolding protein that has at least seven recognizable protein-protein interaction domains. Several complementary approaches were employed to show that the dendrite branching promoting action of full length SAP97 depends on ligand(s) that bind to the PDZ3 domain. Ligand(s) to PDZ1, PDZ2 and I3 domains also contribute to dendrite growth. The ability of PDZ3 ligand(s) to promote dendrite growth depends on localization at the plasma membrane along with GluA1 and SAP97. These results suggest that the assembly of a multi-protein complex at or near synapses is vital for the translation of AMPA-R activity into dendrite growth.

Original language	English (US)
Pages (from-to)	31-44
Number of pages	14
Journal	Molecular and Cellular Neuroscience
Volume	65
DOIs	https://doi.org/10.1016/j.mcn.2015.02.011
State	Published - Mar 1 2015

Funding

The work leading to the studies described herein was supported by US Public Health Service (currently by NS079607-01 and in the past by NS029837 ). The Institutional Intellectual and Developmental Disabilities Research Center P30 HD26979 Cellular Neuroscience Core also provided valuable support for these studies. The authors appreciate the contribution of Weiguo Zhou for the help in the creation of some of the constructs used in these experiments; Ben Margolis for the gift of SAP97 truncation mutants and the technical support from Neha Sharma. Emilia Moscato and Rita Balice-Gordon provided invaluable assistance with the quantitative synaptic image analysis.

Keywords

GluA1
PDZ domain
Spinal cord neuron

ASJC Scopus subject areas

Cellular and Molecular Neuroscience
Molecular Biology
Cell Biology

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10.1016/j.mcn.2015.02.011

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title = "Structure-function analysis of SAP97, a modular scaffolding protein that drives dendrite growth",

abstract = "Activation of AMPA receptors assembled with the GluA1 subunit can promote dendrite growth in a manner that depends on its direct binding partner, SAP97. SAP97 is a modular scaffolding protein that has at least seven recognizable protein-protein interaction domains. Several complementary approaches were employed to show that the dendrite branching promoting action of full length SAP97 depends on ligand(s) that bind to the PDZ3 domain. Ligand(s) to PDZ1, PDZ2 and I3 domains also contribute to dendrite growth. The ability of PDZ3 ligand(s) to promote dendrite growth depends on localization at the plasma membrane along with GluA1 and SAP97. These results suggest that the assembly of a multi-protein complex at or near synapses is vital for the translation of AMPA-R activity into dendrite growth.",

keywords = "GluA1, PDZ domain, Spinal cord neuron",

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AU - Zhang, L.

AU - Hsu, F. C.

AU - Mojsilovic-Petrovic, J.

AU - Jablonski, A. M.

AU - Zhai, J.

AU - Coulter, D. A.

AU - Kalb, R. G.

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N2 - Activation of AMPA receptors assembled with the GluA1 subunit can promote dendrite growth in a manner that depends on its direct binding partner, SAP97. SAP97 is a modular scaffolding protein that has at least seven recognizable protein-protein interaction domains. Several complementary approaches were employed to show that the dendrite branching promoting action of full length SAP97 depends on ligand(s) that bind to the PDZ3 domain. Ligand(s) to PDZ1, PDZ2 and I3 domains also contribute to dendrite growth. The ability of PDZ3 ligand(s) to promote dendrite growth depends on localization at the plasma membrane along with GluA1 and SAP97. These results suggest that the assembly of a multi-protein complex at or near synapses is vital for the translation of AMPA-R activity into dendrite growth.

AB - Activation of AMPA receptors assembled with the GluA1 subunit can promote dendrite growth in a manner that depends on its direct binding partner, SAP97. SAP97 is a modular scaffolding protein that has at least seven recognizable protein-protein interaction domains. Several complementary approaches were employed to show that the dendrite branching promoting action of full length SAP97 depends on ligand(s) that bind to the PDZ3 domain. Ligand(s) to PDZ1, PDZ2 and I3 domains also contribute to dendrite growth. The ability of PDZ3 ligand(s) to promote dendrite growth depends on localization at the plasma membrane along with GluA1 and SAP97. These results suggest that the assembly of a multi-protein complex at or near synapses is vital for the translation of AMPA-R activity into dendrite growth.

KW - GluA1

KW - PDZ domain

KW - Spinal cord neuron

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Structure-function analysis of SAP97, a modular scaffolding protein that drives dendrite growth

Abstract

Funding

Keywords

ASJC Scopus subject areas

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