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Mol Cell Neurosci. 2015 Mar;65:31-44. doi: 10.1016/j.mcn.2015.02.011. Epub 2015 Feb 19.

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

Author information

1
Department of Pediatrics, Division of Neurology, Research Institute, Children's Hospital of Philadelphia, 3615 Civic Center Boulevard, Philadelphia, PA 19104, United States. Electronic address: ZHANGL@email.chop.edu.
2
Department of Pediatrics, Division of Neurology, Research Institute, Children's Hospital of Philadelphia, 3615 Civic Center Boulevard, Philadelphia, PA 19104, United States. Electronic address: HSUF@email.chop.edu.
3
Department of Pediatrics, Division of Neurology, Research Institute, Children's Hospital of Philadelphia, 3615 Civic Center Boulevard, Philadelphia, PA 19104, United States. Electronic address: PETROVIC@email.chop.edu.
4
Department of Neuroscience, Perelman School of Medicine, University of Pennsylvania, 3400 Spruce Street, Philadelphia, PA 19104, United States. Electronic address: ajablo@mail.med.upenn.edu.
5
Department of Pediatrics, Division of Neurology, Research Institute, Children's Hospital of Philadelphia, 3615 Civic Center Boulevard, Philadelphia, PA 19104, United States. Electronic address: zhaijb@yahoo.com.
6
Department of Pediatrics, Division of Neurology, Research Institute, Children's Hospital of Philadelphia, 3615 Civic Center Boulevard, Philadelphia, PA 19104, United States; Department of Neuroscience, Perelman School of Medicine, University of Pennsylvania, 3400 Spruce Street, Philadelphia, PA 19104, United States; Department of Neurology, Perelman School of Medicine, University of Pennsylvania, 3400 Spruce Street, Philadelphia, PA 19104, United States. Electronic address: COULTERD@email.chop.edu.
7
Department of Pediatrics, Division of Neurology, Research Institute, Children's Hospital of Philadelphia, 3615 Civic Center Boulevard, Philadelphia, PA 19104, United States; Department of Neurology, Perelman School of Medicine, University of Pennsylvania, 3400 Spruce Street, Philadelphia, PA 19104, United States. Electronic address: kalb@email.chop.edu.

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

PMID:
25701814
PMCID:
PMC4393785
DOI:
10.1016/j.mcn.2015.02.011
[Indexed for MEDLINE]
Free PMC Article

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