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Published online
doi:10.1083/jcb.200807033
The Journal of Cell Biology, Vol. 184, No. 3, 423-435
The Rockefeller University Press, 0021-9525 $30.00
© di Penta et al.
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Article

Dendritic LSm1/CBP80-mRNPs mark the early steps of transport commitment and translational control



Alessandra di Penta1, Valentina Mercaldo1,2,3, Fulvio Florenzano1, Sebastian Munck2,3, M. Teresa Ciotti4, Francesca Zalfa1,5, Delio Mercanti4, Marco Molinari1, Claudia Bagni1,2,3,5, and Tilmann Achsel1,2,3

1 Laboratory for Neurobiochemistry, Laboratory for Molecular and Cellular Neurobiology, and Laboratory for Neuroanatomy, Department for Experimental Neurosciences, Fondazione Santa Lucia, Istituto di Ricovero e Cura a Carattere Scientifico, 00143 Rome, Italy
2 Center for Human Genetics, Katholieke Universiteit Leuven, and 3 Department of Molecular and Developmental Genetics, Flanders Institute for Biotechnology (VIB), B-3000 Leuven, Belgium
4 Institute for Neurobiology, Consiglio Nazionale delle Ricerche, 00143 Rome, Italy
5 Department of Experimental Medicine and Biochemical Sciences, Faculty of Medicine, University of Rome "Tor Vergata," 00133 Rome, Italy

Correspondence to Tilmann Achsel: Tilmann.Achsel{at}med.kuleuven.be

Messenger RNA (mRNA) transport to neuronal dendrites is crucial for synaptic plasticity, but little is known of assembly or translational regulation of dendritic messenger ribonucleoproteins (mRNPs). Here we characterize a novel mRNP complex that is found in neuronal dendrites throughout the central nervous system and in some axonal processes of the spinal cord. The complex is characterized by the LSm1 protein, which so far has been implicated in mRNA degradation in nonneuronal cells. In brain, it associates with intact mRNAs. Interestingly, the LSm1-mRNPs contain the cap-binding protein CBP80 that associates with (pre)mRNAs in the nucleus, suggesting that the dendritic LSm1 complex has been assembled in the nucleus. In support of this notion, neuronal LSm1 is partially nuclear and inhibition of mRNA synthesis increases its nuclear localization. Importantly, CBP80 is also present in the dendrites and both LSm1 and CBP80 shift significantly into the spines upon stimulation of glutamergic receptors, suggesting that these mRNPs are translationally activated and contribute to the regulated local protein synthesis.


A. di Penta and V. Mercaldo contributed equally to this paper.

A. di Penta's present address is Laboratory for Neuroimmunology, Center for Applied Medical Research, University of Navarra, 31080 Pamplona, Spain.

Abbreviations used in this paper: ActD, actinomycin D; CPEB, cytoplasmic polyadenylation element binding; DHPG, (S)-3,5-dihydroxyphenylglycine; DIV, days in vitro; mRNP, messenger RNP; NF-H, neurofilament heavy chain; SMN, survival of motor neurons.

© 2009 di Penta et al.
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