JCB logo
Accuri Cytometers
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 11 October 2004. doi:10.1083/jcb.200406020
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 167, Number 1, 43-50
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 3849K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Morgan, J. R.
Right arrow Articles by De Camilli, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Morgan, J. R.
Right arrow Articles by De Camilli, P.
Related Collections
Right arrowRelated Article
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Report

A role for talin in presynaptic function



Jennifer R. Morgan1,2, Gilbert Di Paolo1,2, Hauke Werner1,2, Valentina A. Shchedrina1,2, Marc Pypaert1, Vincent A. Pieribone3,4, and Pietro De Camilli1,2

1 Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06519
2 Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06519
3 Department of Physiology, Yale University School of Medicine, New Haven, CT 06519
4 John B. Pierce Laboratory, Yale University School of Medicine, New Haven, CT 06519

Correspondence to Pietro De Camilli: pietro.decamilli{at}yale.edu


Abstract

Talin, an adaptor between integrin and the actin cytoskeleton at sites of cell adhesion, was recently found to be present at neuronal synapses, where its function remains unknown. Talin interacts with phosphatidylinositol-(4)-phosphate 5-kinase type I{gamma}, the major phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P2]–synthesizing enzyme in brain. To gain insight into the synaptic role of talin, we microinjected into the large lamprey axons reagents that compete the talin–PIP kinase interaction and then examined their effects on synaptic structure. A dramatic decrease of synaptic actin and an impairment of clathrin-mediated synaptic vesicle endocytosis were observed. The endocytic defect included an accumulation of clathrin-coated pits with wide necks, as previously observed after perturbing actin at these synapses. Thus, the interaction of PIP kinase with talin in presynaptic compartments provides a mechanism to coordinate PI(4,5)P2 synthesis, actin dynamics, and endocytosis, and further supports a functional link between actin and clathrin-mediated endocytosis.

Abbreviations used in this paper: FERM, band 4.1/ezrin/radixin/moesin-like; ITC, isothermal titration calorimetry; PI(4,5)P2, phosphatidylinositol-(4,5)-bisphosphate; PIPKI{gamma}, phosphatidylinositol-(4)-phosphate 5-kinase type I{gamma}.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?

Related Article

Talin for presynaptic endocytosis
Nicole LeBrasseur
J. Cell Biol. 2004 167: 12-13. [Full Text] [PDF]



This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents