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14-3-3 Proteins in Brain function

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Handbook of Neurochemistry and Molecular Neurobiology

Abstract:

14‐3‐3 proteins were discovered by Moore and Perez in the soluble extract of bovine brain in 1967. These proteins are highly abundant in the brain. In this chapter, the discovery of 14‐3‐3 protein, the structure of 14‐3‐3, the cloning of 14‐3‐3 complementary DNA (cDNA), the nucleotide sequence of 14‐3‐3 cDNA, the structure of the 14‐3‐3 gene, the occurrence of 14‐3‐3 messenger RNA (mRNA) in the brain, the function and regulation of 14‐3‐3 protein, the binding of 14‐3‐3 protein to other proteins, the effects of 14‐3‐3 on the binding of one protein to another, the effects of 14‐3‐3 on protein kinase, and the neuropathology of 14‐3‐3 are described concisely.

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Abbreviations

AD:

Alzheimer's disease

ALS:

amyotrophic lateral sclerosis

ASK:

apoptosis signal‐regulating kinase

BAD:

Bel‐xL/Bel‐2‐associated death promoter

cAMP:

cyclic adenosine monophosphate

CBP:

CREB‐binding protein

Cdc:

cell division cycle

C. elegans :

Caenorhabditis elegans

CRE:

cAMP response element

CJD:

Creutzfeldt–Jakob disease

CSF:

cerebrospinal fluid

cTAK:

Cdc25c‐associated kinase

DEAE cellulose:

diethylaminoethyl cellulose

DLBD:

diffuse Lewy body disorder

FISH:

fluorescence in situ hybridization

FKALR1:

forkhead transcription factor

GSK3β:

glycogen synthase kinase‐3β

HPLC:

high‐performance liquid chromatography

JNK:

C‐JunNH(2) terminal kinase

KLC:

kinesin light chain

KSR:

kinase suppressor of ras

LTP:

long‐term potentiation

MS/MS:

tandem mass spectrometry

mRNA:

messenger ribonucleic acid

NFTs:

neurofibrillary tangles

PCR:

polymerase chain reaction

PC12:

pheochromocytoma cell 12

Poly(A):

polyadenylic acid

PD:

Parkinson's disease

PKC:

protein kinase C

SCA1:

spinocerebellar ataxia type 1

SDK1:

sphingosine‐dependent protein kinase 1

SDS‐PAGE:

sodium dodecylsulfate‐polyacrylamide gel electrophoresis

TAB:

TATA‐binding protein

TAFII:

TAB‐associated factor II

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Acknowledgments

The author heartily thanks Prof. George Hauser (Ralph Lowell Laboratories, McLean Hospital, Belmont, MA 02378, USA) for his kind reading and correction of the manuscript. Table 12-2 was used with the permission of Dr. D. Berg. The author heartily thanks Dr. D. Berg (Institute for Medical Genetics, University of Tübingen, Tübingen, Germany). Figure 4 was used under the permission of Nature Editorial Office. The author heartily thanks Nature Editorial Office. The author heartily thanks Dr. K. Washiyama (Department of Molecular Neuropathology, Brain Research Institute, Niigata University, Niigata, Japan) for his kind support during the writing of this review.

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  1. Y. Takahashi
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Editors and Affiliations

  1. Center for Neurochemistry, Nathan S. Kline Institute for Psychiatric Research, 140 Old Orangeburg Road, 10962, Orangeburg, Newyork, USA

    Abel Lajtha (Director) (Director)

  2. Department of Neurology (Division of Neurochemistry and Neurobiology), University of Iowa College of Medicine and Veterans Administration Medical Center, 52242, lowa, lowa, USA

    Ramon Lim

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© 2006 Springer Science+Business Media, LLC

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Takahashi, Y. (2006). 14-3-3 Proteins in Brain function. In: Lajtha, A., Lim, R. (eds) Handbook of Neurochemistry and Molecular Neurobiology. Springer, Boston, MA. https://doi.org/10.1007/978-0-387-30381-9_12

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