QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

HOME  |   SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

The Journal of Neuroscience, August 5, 2009, 29(31):9778-9793; doi:10.1523/JNEUROSCI.2613-09.2009

This Article Full Text Full Text (PDF) Supplemental Data Submit an eLetter Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Sebeo, J. Articles by Benson, D. L. Search for Related Content PubMed PubMed Citation Articles by Sebeo, J. Articles by Benson, D. L.

 Previous Article  |  Next Article 

Development/Plasticity/Repair
Requirement for Protein Synthesis at Developing Synapses

Joseph Sebeo,¹ Kuangfu Hsiao,^1 * Ozlem Bozdagi,^1 * Dani Dumitriu,¹ Yongchao Ge,² Qiang Zhou,² and Deanna L. Benson¹

¹Fishberg Department of Neuroscience and ²Department of Neurology, Mount Sinai School of Medicine, New York, New York 10029

Correspondence should be addressed to Deanna L. Benson, Fishberg Department of Neuroscience, Mount Sinai School of Medicine, 1425 Madison Avenue, Box 1065, New York, NY 10029. Email: deanna.benson{at}mssm.edu

Activity and protein synthesis act cooperatively to generate persistent changes in synaptic responses. This forms the basis for enduring memory in adults. Activity also shapes neural circuits developmentally, but whether protein synthesis plays a congruent function in this process is poorly understood. Here, we show that brief periods of global or local protein synthesis inhibition decrease the synaptic vesicles available for fusion and increase synapse elimination. Ca²⁺/calmodulin-dependent protein kinase II (CaMKII) is a critical target; its levels are controlled by rapid turnover, and blocking its activity or knocking it down recapitulates the effects of protein synthesis inhibition. Mature presynaptic terminals show decreased sensitivity to protein synthesis inhibition, and resistance coincides with a developmental switch in regulation from CaMKII to PKA (protein kinase A). These findings demonstrate a novel mechanism regulating presynaptic activity and synapse elimination during development, and suggest that protein translation acts coordinately with activity to selectively stabilize appropriate synaptic interactions.

---

Received June 4, 2009; accepted June 15, 2009.

Correspondence should be addressed to Deanna L. Benson, Fishberg Department of Neuroscience, Mount Sinai School of Medicine, 1425 Madison Avenue, Box 1065, New York, NY 10029. Email: deanna.benson{at}mssm.edu

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help