Cerebral Cortex Advance Access originally published online on March 9, 2005
Cerebral Cortex 2005 15(12):1928-1937; doi:10.1093/cercor/bhi070
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Differential Localization of Protein Phosphatase-1
, ß and 
1 Isoforms in Primate Prefrontal Cortex
1 Division of Neuroscience, Yerkes National Primate Research Center, Atlanta, GA, USA, 2 Department of Neurology, Emory University, Atlanta, GA, USA, 3 Department of Psychiatry, Yale University School of Medicine, New Haven, CT, USA, 4 Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, 1230 York Ave, New York, NY, USA, 5 Department of Molecular Physiology & Biophysics, Vanderbilt University School of Medicine, Nashville, TN, USA and 6 Department of Psychiatry and Behavioral Sciences, Emory University, Atlanta, GA, USA
Address correspondence to E. Chris Muly, Yerkes National Primate Research Center, 954 Gatewood Rd NE, Atlanta, GA 30322, USA. Email: ecmuly{at}rmy.emory.edu.
Prefrontal cortical functioning depends on D1 family receptors and their complex signal transduction cascade, including protein phosphatase-1 (PP1). Three PP1 isoforms are prominent in the brain: PP1
, PP1ß and PP1
1. PP1 localization by a variety of scaffolding proteins is critical for dopamine-mediated modulation of glutamatergic neurotransmission. We have quantified the subcellular distribution of each isoform in primate prefrontal cortex using immunoelectron microscopy. All three are found in spines, dendrites, axon terminals, axons and glia. However, PP1 and PP11 labeling is enriched in spines, whereas PP1ß label is enriched in dendrites. Using post-embedding immunogold labeling, we further examined the distribution of PP1 and PP11 within spines. PP11 is highly and specifically concentrated in the postsynaptic density (PSD) of these spines, while PP1 is enriched in the PSD but also found subjacent to the PSD in moderate amounts. Thus, PP1 isoforms are heterogeneously distributed in the cortical neuropil and within spines. These results suggest that each PP1 isoform has access to a different set of substrates and, furthermore, they demonstrate that the composition of signal transduction proteins varies in different parts of the neuron and even in different regions of a dendritic spine in the primate PFC.
Key Words: electron microscopy • post-embedding immunogold • postsynaptic density • scaffolding protein • signal transduction
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  L. C. Carmody, A. J. Baucum II, M. A. Bass, and R. J. Colbran Selective targeting of the {gamma}1 isoform of protein phosphatase 1 to F-actin in intact cells requires multiple domains in spinophilin and neurabin FASEB J, June 1, 2008; 22(6): 1660 - 1671. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. M. Brown, A. J. Baucum, M. A. Bass, and R. J. Colbran Association of Protein Phosphatase 1{gamma}1 with Spinophilin Suppresses Phosphatase Activity in a Parkinson Disease Model J. Biol. Chem., May 23, 2008; 283(21): 14286 - 14294. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. Novoyatleva, B. Heinrich, Y. Tang, N. Benderska, M. E.R. Butchbach, C. L. Lorson, M. A. Lorson, C. Ben-Dov, P. Fehlbaum, L. Bracco, et al. Protein phosphatase 1 binds to the RNA recognition motif of several splicing factors and regulates alternative pre-mRNA processing Hum. Mol. Genet., January 1, 2008; 17(1): 52 - 70. [Abstract] [Full Text] [PDF]
|
|