Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2012;3(2):152-64.
Epub 2012 May 18.

14-3-3 proteins in neurological disorders

Molly Foote  1 , Yi Zhou
Affiliations

14-3-3 proteins in neurological disorders

Molly Foote et al. Int J Biochem Mol Biol. 2012.

Abstract

14-3-3 proteins were originally discovered as a family of proteins that are highly expressed in the brain. Through interactions with a multitude of binding partners, 14-3-3 proteins impact many aspects of brain function including neural signaling, neuronal development and neuroprotection. Although much remains to be learned and understood, 14-3-3 proteins have been implicated in a variety of neurological disorders based on evidence from both clinical and laboratory studies. Here we will review previous and more recent research that has helped us understand the roles of 14-3-3 proteins in both neurodegenerative and neuropsychiatric diseases.

Keywords: 14-3-3; neurodegenerative diseases; neurodevelopment; neuropsychiatric diseases.

PubMed Disclaimer

Figures

Figure 1
Figure 1
The Ndel1/Lis1/14-3-3ε Protein Complex for Neurite Outgrowth. 14-3-3ε binds to phosphorylated Ndel1 to promote the formation of the Ndel1/Lis1 protein complex. This protein complex binds to DISC1 and is then translocated to the axonal growth cone for cytoskeletal reorganization. Abbreviations: AF, actin filaments; MT, mircotubules; P, phosphorylation.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Aitken A. 14-3-3 proteins on the MAP. Trends Biochem Sci. 1995;20:95–97. - PubMed
    1. Rosenquist M, Sehnke P, Ferl RJ, Sommarin M, Larsson C. Evolution of the 14-3-3 protein family: does the large number of isoforms in multicellular organisms reflect functional specificity? J Mol Evol. 2000;51:446–458. - PubMed
    1. Liu D, Bienkowska J, Petosa C, Collier RJ, Fu H, Liddington R. Crystal structure of the zeta isoform of the 14-3-3 protein. Nature. 1995;376:191–194. - PubMed
    1. Xiao B, Smerdon SJ, Jones DH, Dodson GG, Soneji Y, Aitken A, Gamblin SJ. Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways. Nature. 1995;376:188–191. - PubMed
    1. Rittinger K, Budman J, Xu J, Volinia S, Cantley LC, Smerdon SJ, Gamblin SJ, Yaffe MB. Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding. Mol Cell. 1999;4:153–166. - PubMed

LinkOut - more resources