Standing out in the field of IgY Immunotechnology

  • Home
    Home A full collection of all the Research Archive entries.
  • Years
    Years Sort entries by year.
  • Tags
    Tags Displays a list of tags that have been used in the blog.
  • Archives
    Archives Contains a list of research entries that were created previously.

The novel synaptogenic protein Farp1 links postsynaptic cytoskeletal dynamics and transsynaptic organization.*

Posted by on in 2012
  • Font size: Larger Smaller
  • Hits: 2899
  • Print
Cheadle LBiederer T. 2012. J Cell Biol. 199:985-1001. doi: 10.1083/jcb.201205041. Epub 2012 Dec 3.

Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520.


Synaptic adhesion organizes synapses, yet the signaling pathways that drive and integrate synapse development remain incompletely understood. We screened for regulators of these processes by proteomically analyzing synaptic membranes lacking the synaptogenic adhesion molecule SynCAM 1. This identified FERM, Rho/ArhGEF, and Pleckstrin domain protein 1 (Farp1) as strongly reduced in SynCAM 1 knockout mice. Farp1 regulates dendritic filopodial dynamics in immature neurons, indicating roles in synapse formation. Later in development, Farp1 is postsynaptic and its 4.1 protein/ezrin/radixin/moesin (FERM) domain binds SynCAM 1, assembling a synaptic complex. Farp1 increases synapse number and modulates spine morphology, and SynCAM 1 requires Farp1 for promoting spines. In turn, SynCAM 1 loss reduces the ability of Farp1 to elevate spine density. Mechanistically, Farp1 activates the GTPase Rac1 in spines downstream of SynCAM 1 clustering, and promotes F-actin assembly. Farp1 furthermore triggers a retrograde signal regulating active zone composition via SynCAM 1. These results reveal a postsynaptic signaling pathway that engages transsynaptic interactions to coordinate synapse development.

*Note: The anti-IgY agarose used in this publication was manufactured by Gallus Immunotech Inc.


Last modified on