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Regulation of Protein Metabolism

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Handbook of Neurochemistry and Molecular Neurobiology

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Abstract:

Translation is a sophisticated and complex mechanism requiring extensive biological machinery and subjected to an extremely fine regulation. Given that proteins account for a large fraction of biological macromolecules, a large proportion of the resource of cells is devoted to translation. Translation can be broken into three stages: initiation, elongation, termination. Regulation of translation can be exerted at many levels but in the first step, structural features in mRNAs in concert with the interactions among the initiation factors and other regulatory proteins, offer the possibility to regulate protein synthesis in rapid response to external stimuli, without invoking nuclear pathways for mRNA synthesis. The range of biological process that involve translational control of gene expression is expanding, in the brain, recent reports have provided evidences of the importance of translational control in process such us ischemia and reperfusion, neuronal plasticity and memory.

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Abbreviations

AMPA:

alpha-amino-3-hydroxy-5methyl-4-isoxazolepropionic acid

ATF4:

activating transcription factor 4

AUG:

initiation codons

Cdk5:

cyclin-dependent kinase 5

4EBPs:

initiation factor 4E binding protein family

eEFs:

eukaryotic elongation factors

eIFs:

eukaryotic initiation factors

eIF2α:

the α subunit of initiation factor 2

eIF2(αP):

the phosphorylated form of eIF2α

ER:

endoplasmic reticulum

ERK:

extracellular signal-regulated kinase

GADD34:

growth arrest and DNA damage protein 34

GCN2:

general control nonderepressible-2 kinase

GluR2:

glutamate receptor 2 subunit of AMPA receptor

GRP78:

glucose-regulated protein of 78 kDa

GSK-3:

glycogen synthase kinase-3

HRI:

heme-regulated inhibitor

IRES:

internal ribosome entry sites

Met-tRNAi :

initiator methionyl transfer RNA

m7G cap:

5′-m7G(5′)ppp(5′)N cap structure

Mnk:

MAP kinase-interacting kinase

mTOR:

target of rapamycin

NR2A:

the N-metyl-D-aspartate (NMDA) receptor subunit 2A

uORF:

upstream open reading frame

PABP:

poly(A)-binding proteins

PKR:

the double-stranded RNA-dependent kinase

PERK:

mammalian ER resident kinase

PI3K/Akt-PKB:

phosphatidylinositol-3-kinase/phosphatidylinositol-3-kinase-protein B

poly (A):

3′-polyadenylated tail

PP1c:

catalytic subunit of protein phosphatase 1

S6K1/2:

ribosomal protein S6 kinase 1/2

5′TOP:

terminal oligopyrimidine tracts

UPR:

unfolded protein response

UTR:

untranslated region

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Acknowledgments

We apologize to investigators whose work was not cited or discussed in detail due to space limitations. We want to thank our collaborators Alberto Alcázar, Juan L. Fando, M. Elena Martín, and Victor M. González for valuable suggestions and the critical reading of this chapter. We are also indebted to our fellows, Milina Hrehorovská, Lidia García, Cristina Martín de la Vega, Francisco Muñoz, Celia Quevedo, and Ana O'Loghlen, for the excellent work performed in the last years. Work from the authors’ own laboratory was supported by grants FIS 02/0304 and 05/0312 (Ministerio de Sanidad y Consumo) and SK-VEGA 2/3219/23 (Slovak Academy of Sciences).

Authors
  1. M. Salinas
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  2. J. Burda
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Editors and Affiliations

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

    Abel Lajtha (Director) (Director)

  2. Department of Neurosciences Division of Neurology, Medical University of South Carolina, 96 Jonathan Lucas Street Suite 309, Charleston, SC 29425, USA

    Naren Banik (Professor) (Professor)

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© 2007 Springer Science+Business Media, LLC

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Salinas, M., Burda, J. (2007). Regulation of Protein Metabolism. In: Lajtha, A., Banik, N. (eds) Handbook of Neurochemistry and Molecular Neurobiology. Springer, Boston, MA. https://doi.org/10.1007/978-0-387-30379-6_1

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