WWW.JNEUROSCI.ORG
-
The Journal of Neuroscience
 QUICK SEARCH:   [advanced]


     
-


HOME
  |  
SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

The Journal of Neuroscience, May 28, 2008, 28(22):5654-5659; doi:10.1523/JNEUROSCI.0756-08.2008

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Data
Right arrow Submit an eLetter
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Related articles in J. Neurosci.
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Web of Science (1)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rácz, B.
Right arrow Articles by Weinberg, R. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rácz, B.
Right arrow Articles by Weinberg, R. J.

 Previous Article  |  Next Article 

Brief Communications
Organization of the Arp2/3 Complex in Hippocampal Spines

Bence Rácz1 and Richard J. Weinberg2

1Department of Anatomy and Histology, Faculty of Veterinary Science, Szent István University, 1078 Budapest, Hungary, and 2Department of Cell and Developmental Biology, and Neuroscience Center, University of North Carolina, Chapel Hill, North Carolina 27599-7090

Correspondence should be addressed to Bence Rácz, Szent Istvan University, István u. 2, 1078 Budapest, Hungary. Email: racz.bence{at}aotk.szie.hu

Changes in the morphology of a dendritic spine require remodeling of its actin-based cytoskeleton. Biochemical mechanisms underlying actin remodeling have been studied extensively, but little is known about the physical organization of the actin-binding proteins that mediate remodeling in spines. Long-term potentiation-inducing stimuli trigger expansion of the spine head, suggesting local extension and branching of actin filaments. Because filament branching requires the Arp2/3 complex, we used quantitative immunoelectron microscopy to elucidate the organization of ARPC-2 (Arp2/3 complex subunit 2), an essential component of the complex. Our data from CA1 hippocampus indicate that Arp2/3 concentrates within spines in a previously unrecognized torroidal domain, apparently specialized to mediate actin filament branching.

Key words: actin; cytoskeleton; hippocampus; LTP; pyramidal cell; synaptic plasticity


Received Feb. 19, 2008; revised April 17, 2008; accepted April 20, 2008.

Correspondence should be addressed to Bence Rácz, Szent Istvan University, István u. 2, 1078 Budapest, Hungary. Email: racz.bence{at}aotk.szie.hu


Related articles in J. Neurosci.:

This Week in The Journal

J. Neurosci. 2008 28: i. [Full Text]  





-
-

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help

-
Copyright 2009 by Society for Neuroscience ONLINE ISSN: 1529-2401
-