A Novel Role for Snapin in Dendrite Patterning: Interaction with Cypin
-
Published:2005-11
Issue:11
Volume:16
Page:5103-5114
-
ISSN:1059-1524
-
Container-title:Molecular Biology of the Cell
-
language:en
-
Short-container-title:MBoC
Author:
Chen Maxine12, Lucas Kenyatta G.13, Akum Barbara F.12, Balasingam Gaithri1, Stawicki Tamara M.1, Provost Janine M.1, Riefler Gary M.1, Jörnsten Rebecka J.4, Firestein Bonnie L.1
Affiliation:
1. Department of Cell Biology and Neuroscience, Rutgers University, Piscataway, NJ 08854-8082 2. Molecular Biosciences, Rutgers University, Piscataway, NJ 08854-8082 3. Neurobiology Graduate Programs, Rutgers University, Piscataway, NJ 08854-8082 4. Department of Statistics, Rutgers University, Piscataway, NJ 08854-8082
Abstract
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, collapsin response mediator protein (CRMP) homology, and PSD-95, Discs large, zona occludens-1 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. Together, our data suggest that snapin regulates dendrite number in developing neurons by modulating cypin-promoted microtubule assembly.
Publisher
American Society for Cell Biology (ASCB)
Subject
Cell Biology,Molecular Biology
Reference47 articles.
1. Aizawa, H., Hu, S. C., Bobb, K., Balakrishnan, K., Ince, G., Gurevich, I., Cowan, M., and Ghosh, A. (2004). Dendrite development regulated by CREST, a calcium-regulated transcriptional activator. Science 303, 197–202. 2. Akum, B. F., Chen, M., Gunderson, S. I., Riefler, G. M., Scerri-Hansen, M. M., and Firestein, B. L. (2004). Cypin regulates dendrite patterning in hippocampal neurons by promoting microtubule assembly. Nat. Neurosci. 7, 145–152. 3. Audesirk, G., Cabell, L., and Kern, M. (1997). Modulation of neurite branching by protein phosphorylation in cultured rat hippocampal neurons. Brain Res. Dev. Brain Res. 102, 247–260. 4. Audesirk, T., Cabell, L., Kern, M., and Audesirk, G. (2003a). beta-estradiol influences differentiation of hippocampal neurons in vitro through an estrogen receptor-mediated process. Neuroscience 121, 927–934. 5. Audesirk, T., Cabell, L., Kern, M., and Audesirk, G. (2003b). Enhancement of dendritic branching in cultured hippocampal neurons by 17beta-estradiol is mediated by nitric oxide. Int. J. Dev. Neurosci. 21, 225–233.
Cited by
47 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
|
|