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MBC in Press, published online ahead of print August 24, 2005
Mol. Biol. Cell 10.1091/mbc.E05-02-0165

A more recent version of this article appeared on November 1, 2005 Originally published as MBC in Press, 10.1091/mbc.E05-02-0165 on August 24, 2005
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Submitted on February 25, 2005
Accepted on August 11, 2005

A Novel Role for Snapin in Dendrite Patterning: Interaction with Cypin

Maxine Chen,*{dagger}{ddagger} Kenyatta G. Lucas,*{ddagger}{sect} Barbara F. Akum,*{dagger} Gaithri Balasingam,* Tamara M. Stawicki,* Janine M. Provost,* Gary M. Riefler,* Rebecka J. Jörnsten,|| and Bonnie L. Firestein*

*Department of Cell Biology and Neuroscience, {dagger}Molecular Biosciences and {sect}Neurobiology Graduate Programs, and ||Department of Statistics, Rutgers University, Piscataway, NJ 08854-8082

Monitoring Editor: Erika Holzbaur

Temporal and spatial assembly of signal transduction machinery determines dendrite branch patterning, a process crucial for proper synaptic transmission. Our laboratory previously cloned and characterized cypin, a protein that decreases PSD-95 family member localization and regulates dendrite number. Cypin contains zinc binding, CRMP homology, and PDZ binding domains. Both the zinc binding and CRMP homology domains are needed for dendrite patterning. In addition, cypin binds tubulin via its CRMP homology domain to promote microtubule assembly. Using a yeast two-hybrid screen of a rat brain cDNA library with cypin lacking the carboxyl terminal eight amino acids as bait, we identified snapin as a cypin binding partner. Here we show by affinity chromatography and coimmunoprecipitation that the carboxyl-terminal coiled-coil domain (H2) of snapin is required for cypin binding. In addition, snapin binds to cypin’s CRMP homology domain, which is where tubulin binds. We also show that snapin competes with tubulin for binding to cypin, resulting in decreased microtubule assembly. Subsequently, overexpression of snapin in primary cultures of hippocampal neurons results in decreased primary dendrites present on these neurons and increased probability of branching. Taken together, our data suggest that snapin regulates dendrite number in developing neurons by modulating cypin-promoted microtubule assembly.

{ddagger}These authors contributed equally to this work.




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