scholarly journals Asymmetrical β-actin mRNA translation in growth cones mediates attractive turning to netrin-1

2006 ◽  
Vol 9 (10) ◽  
pp. 1247-1256 ◽  
Author(s):  
Kin-Mei Leung ◽  
Francisca PG van Horck ◽  
Andrew C Lin ◽  
Rachel Allison ◽  
Nancy Standart ◽  
...  
Keyword(s):  
Mrna Translation ◽  
Growth Cones ◽  
Actin Mrna

scholarly journals Visualization of mRNA translation in living cells

2006 ◽  
Vol 175 (1) ◽  
pp. 67-76 ◽  
Author(s):  
Alexis J. Rodriguez ◽  
Shailesh M. Shenoy ◽  
Robert H. Singer ◽  
John Condeelis
Keyword(s):  
Mrna Translation ◽  
Leading Edge ◽  
Intercellular Junctions ◽  
Mrna Localization ◽  
Living Cells ◽  
C2c12 Cells ◽  
Cell Periphery ◽  
Actin Mrna ◽  
Cell Asymmetry ◽  
Cellular Compartments

The role of mRNA localization is presumably to effect cell asymmetry by synthesizing proteins in specific cellular compartments. However, protein synthesis has never been directly demonstrated at the sites of mRNA localization. To address this, we developed a live cell method for imaging translation of β-actin mRNA. Constructs coding for β-actin, containing tetracysteine motifs, were transfected into C2C12 cells, and sites of nascent polypeptide chains were detected using the biarsenial dyes FlAsH and ReAsH, a technique we call translation site imaging. These sites colocalized with β-actin mRNA at the leading edge of motile myoblasts, confirming that they were translating. β-Actin mRNA lacking the sequence (zipcode) that localizes the mRNA to the cell periphery, eliminated the translation there. A pulse-chase experiment on living cells showed that the recently synthesized protein correlated spatially with the sites of its translation. Additionally, localization of β-actin mRNA and translation activity was enhanced at cell contacts and facilitated the formation of intercellular junctions.

Stimulation of myofibrillar synthesis by exercise is mediated by more efficient translation of mRNA

1999 ◽  
Vol 86 (4) ◽  
pp. 1220-1225 ◽  
Author(s):  
Stephen Welle ◽  
Kirti Bhatt ◽  
Charles A. Thornton
Keyword(s):  
Protein Synthesis ◽  
Resistance Exercise ◽  
Vastus Lateralis ◽  
Mrna Translation ◽  
Human Muscle ◽  
Total Rna ◽  
Resistance Exercises ◽  
Actin Mrna ◽  
Membrane Hybridization ◽  
Stimulation Of

Resistance exercises stimulate protein synthesis in human muscle, but the roles of changes in mRNA concentrations and changes in the efficiency of mRNA translation have not been defined. The present study was done to determine whether resistance exercise affects concentrations of total RNA, total mRNA, actin mRNA, or myosin heavy-chain mRNA (total and isoform specific). Eight subjects, 62–75 yr old, performed unilateral knee extensions at 80% of their one-repetition-maximum capacity on days 1, 3, and 6 of the study. On day 7, biopsies of exercised and nonexercised vastus lateralis muscles were obtained. Myofibrillar synthesis was determined by stable- isotope incorporation, and mRNA concentrations were determined by membrane hybridization and PCR-based methods. The exercise stimulated myofibrillar synthesis [30 ± 6 (SE)%] without affecting RNA or mRNA concentrations. The effect of exercise on protein synthesis in individual subjects did not correlate with the effect on total RNA and mRNA concentrations. These data suggest that the stimulation of myofibrillar synthesis by resistance exercise is mediated by more efficient translation of mRNA.

scholarly journals RACK1 is required for axon guidance and local translation at growth cone point contacts

2019 ◽  
Author(s):  
Leah Kershner ◽  
Taylor Bumbledare ◽  
Paige Cassidy ◽  
Samantha Bailey ◽  
Kristy Welshhans
Keyword(s):  
Nervous System ◽  
Growth Cone ◽  
Axon Growth ◽  
Growth Cones ◽  
Scaffolding Protein ◽  
Local Translation ◽  
Point Contacts ◽  
Adhesion Sites ◽  
Actin Mrna ◽  
Developing Nervous System

AbstractLocal translation regulates the formation of appropriate connectivity in the developing nervous system. However, the localization and molecular mechanisms underlying this translation within growth cones is not well understood. Receptor for activated C kinase 1 (RACK1) is a multi-functional ribosomal scaffolding protein that interacts with β-actin mRNA. We recently showed that RACK1 localizes to and regulates the formation of point contacts, which are adhesion sites that control growth cone motility. This suggests that local translation occurs at these adhesion sites that are important for axonal pathfinding, but this has not been investigated. Here, we show that RACK1 is required for BDNF-induced local translation of β-actin mRNA in growth cones. Furthermore, the ribosomal binding function of RACK1 regulates point contact formation, and axon growth and guidance. We also find that local translation of β-actin occurs at point contacts. Taken together, we show that adhesions are a targeted site of local translation within growth cones, and RACK1 is critical to the formation of point contacts and appropriate neural development. These data provide further insight into how and where local translation is regulated, and thereby leads to appropriate connectivity formation in the developing nervous system.

Subcellular localization of an intermediate filament protein and its mRNA in glial cells

1989 ◽  
Vol 9 (10) ◽  
pp. 4556-4559
Author(s):  
P V Sarthy ◽  
M Fu ◽  
J Huang
Keyword(s):  
Glial Cell ◽  
Intermediate Filament ◽  
Mrna Translation ◽  
Mrna Localization ◽  
Intermediate Filament Protein ◽  
Cell Cytoplasm ◽  
Distal Process ◽  
Spatially Distributed ◽  
Actin Mrna ◽  
Filament Protein

Eucaryotic mRNAs are generally localized in the cell body, where most protein synthesis occurs. We have found that mRNAs encoding the glial intermediate filament protein are spatially distributed in the glial cell cytoplasm close to the location of the glial filaments. Whereas the glial filament protein mRNA was located predominantly in the distal process, actin mRNA was found almost exclusively in the apical portion of the glial cell. This pattern of mRNA localization might provide a mechanism for synthesis of proteins in specific subcellular compartments by mRNA translation locally.

scholarly journals Neurotrophin Regulation of β-Actin mRNA and Protein Localization within Growth Cones

1999 ◽  
Vol 147 (1) ◽  
pp. 59-70 ◽  
Author(s):  
H.L. Zhang ◽  
R.H. Singer ◽  
G.J. Bassell
Keyword(s):  
Growth Cone ◽  
Neuronal Development ◽  
Protein Localization ◽  
Growth Cones ◽  
Similar Response ◽  
Signaling Mechanism ◽  
Neurotrophin 3 ◽  
Neuronal Processes ◽  
Dependent Protein ◽  
Actin Mrna

Neurotrophins play an essential role in the regulation of actin-dependent changes in growth cone shape and motility. We have studied whether neurotrophin signaling can promote the localization of β-actin mRNA and protein within growth cones. The regulated localization of specific mRNAs within neuronal processes and growth cones could provide a mechanism to modulate cytoskeletal composition and growth cone dynamics during neuronal development. We have previously shown that β-actin mRNA is localized in granules that were distributed throughout processes and growth cones of cultured neurons. In this study, we demonstrate that the localization of β-actin mRNA and protein to growth cones of forebrain neurons is stimulated by neurotrophin-3 (NT-3). A similar response was observed when neurons were exposed to forskolin or db-cAMP, suggesting an involvement of a cAMP signaling pathway. NT-3 treatment resulted in a rapid and transient stimulation of PKA activity that preceded the localization of β-actin mRNA. Localization of β-actin mRNA was blocked by prior treatment of cells with Rp-cAMP, an inhibitor of cAMP-dependent protein kinase A. Depolymerization of microtubules, but not microfilaments, inhibited the NT-3–induced localization of β-actin mRNA. These results suggest that NT-3 activates a cAMP-dependent signaling mechanism to promote the microtubule-dependent localization of β-actin mRNA within growth cones.

scholarly journals Cue-Polarized Transport of β-actin mRNA Depends on 3′UTR and Microtubules in Live Growth Cones

2018 ◽  
Vol 12 ◽  
Author(s):  
Kin-Mei Leung ◽  
Bo Lu ◽  
Hovy Ho-Wai Wong ◽  
Julie Qiaojin Lin ◽  
Benita Turner-Bridger ◽  
...  
Keyword(s):  
Growth Cones ◽  
Actin Mrna ◽  
Polarized Transport

scholarly journals Translation of Human β-Actin mRNA is Regulated by mTOR Pathway

Genes ◽  
2019 ◽  
Vol 10 (2) ◽  
pp. 96 ◽  
Author(s):  
Irina Eliseeva ◽  
Maria Vasilieva ◽  
Lev Ovchinnikov
Keyword(s):  
Ribosomal Proteins ◽  
Kinase Inhibitor ◽  
Mammalian Target Of Rapamycin ◽  
Mrna Translation ◽  
Housekeeping Genes ◽  
Negative Control ◽  
Translation Regulation ◽  
Mtor Kinase ◽  
Mtorc1 Pathway ◽  
Actin Mrna

The mammalian target of rapamycin (mTOR) kinase is a well-known master regulator of growth-dependent gene expression in higher eukaryotes. Translation regulation is an important function of the mTORC1 pathway that controls the synthesis of many ribosomal proteins and translation factors. Housekeeping genes such as β-actin (ACTB) are widely used as negative control genes in studies of growth-dependent translation. Here we demonstrate that translation of both endogenous and reporter ACTB mRNA is inhibited in the presence of mTOR kinase inhibitor (Torin1) and under amino acid starvation. Notably, 5’UTR and promoter of ACTB are sufficient for the mTOR-dependent translational response, and the degree of mTOR-sensitivity of ACTB mRNA translation is cell type-dependent.

Sign in / Sign up

Export Citation Format

Share Document