Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
An Architectural Framework That May Lie at the Core of the Postsynaptic Density
Marisa K. Baron,1Tobias M. Boeckers,2Bianca Vaida,2Salem Faham,1Mari Gingery,1Michael R. Sawaya,1Danielle Salyer,1Eckart D. Gundelfinger,3James U. Bowie1*
The postsynaptic density (PSD) is a complex assembly of proteinsassociated with the postsynaptic membrane that organizes neurotransmitterreceptors, signaling pathways, and regulatory elements withina cytoskeletal matrix. Here we show that the sterile alpha motifdomain of rat Shank3/ProSAP2, a master scaffolding protein locateddeep within the PSD, can form large sheets composed of helicalfibers stacked side by side. Zn2+, which is found in high concentrationsin the PSD, binds tightly to Shank3 and may regulate assembly.Sheets of the Shank protein could form a platform for the constructionof the PSD complex.
1 Department of Chemistry and Biochemistry, Molecular Biology Institute and University of California at Los Angeles–U.S. Department of Energy Institute for Genomics and Proteomics, University of California, Los Angeles, 611 Charles E. Young Drive East, Los Angeles, CA 90095-1570, USA. 2 Institute of Anatomy and Cell Biology, University of Ulm, Ulm, Germany. 3 Leibniz Institute for Neurobiology, Post Office Box 1860, D-39008 Magdeburg, Germany.
* To whom correspondence should be addressed. E-mail: bowie{at}mbi.ucla.edu
Neurobehavioral Profile and Brain Imaging Study of the 22q13.3 Deletion Syndrome in Childhood.
A. Philippe, N. Boddaert, L. Vaivre-Douret, L. Robel, L. Danon-Boileau, V. Malan, M.-C. de Blois, D. Heron, L. Colleaux, B. Golse, et al. (2008)
Pediatrics
122, e376-e382
|Abstract »|Full Text »|PDF »
Phosphorylation of Homer3 by Calcium/Calmodulin-Dependent Kinase II Regulates a Coupling State of Its Target Molecules in Purkinje Cells.
A. Mizutani, Y. Kuroda, A. Futatsugi, T. Furuichi, and K. Mikoshiba (2008)
J. Neurosci.
28, 5369-5382
|Abstract »|Full Text »|PDF »
Organization of the core structure of the postsynaptic density.
X. Chen, C. Winters, R. Azzam, X. Li, J. A. Galbraith, R. D. Leapman, and T. S. Reese (2008)
PNAS
105, 4453-4458
|Abstract »|Full Text »|PDF »
CNK and HYP form a discrete dimer by their SAM domains to mediate RAF kinase signaling.
T. Rajakulendran, M. Sahmi, I. Kurinov, M. Tyers, M. Therrien, and F. Sicheri (2008)
PNAS
105, 2836-2841
|Abstract »|Full Text »|PDF »
Composition of the Synaptic PSD-95 Complex.
A. Dosemeci, A. J. Makusky, E. Jankowska-Stephens, X. Yang, D. J. Slotta, and S. P. Markey (2007)
Mol. Cell. Proteomics
6, 1749-1760
|Abstract »|Full Text »|PDF »
Intrinsic disorder in the C-terminal domain of the Shaker voltage-activated K+ channel modulates its interaction with scaffold proteins.
E. Magidovich, I. Orr, D. Fass, U. Abdu, and O. Yifrach (2007)
PNAS
104, 13022-13027
|Abstract »|Full Text »|PDF »
Maturation of Synaptic Contacts in Differentiating Neural Stem Cells.
S. Liebau, B. Vaida, A. Storch, and T. M. Boeckers (2007)
Stem Cells
25, 1720-1729
|Abstract »|Full Text »|PDF »
Molecular Basis of Gephyrin Clustering at Inhibitory Synapses: ROLE OF G- AND E-DOMAIN INTERACTIONS.
T. Saiyed, I. Paarmann, B. Schmitt, S. Haeger, M. Sola, G. Schmalzing, W. Weissenhorn, and H. Betz (2007)
J. Biol. Chem.
282, 5625-5632
|Abstract »|Full Text »|PDF »
ProSAP-interacting Protein 1 (ProSAPiP1), a Novel Protein of the Postsynaptic Density That Links the Spine-associated Rap-Gap (SPAR) to the Scaffolding Protein ProSAP2/Shank3.
D. Wendholt, C. Spilker, A. Schmitt, A. Dolnik, K.-H. Smalla, C. Proepper, J. Bockmann, K. Sobue, E. D. Gundelfinger, M. R. Kreutz, et al. (2006)
J. Biol. Chem.
281, 13805-13816
|Abstract »|Full Text »|PDF »
