Click here to close
Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly.
We suggest using a current version of Chrome,
FireFox, or Safari.
Cell
2003 Dec 26;1157:893-904. doi: 10.1016/s0092-8674(03)01021-3.
Show Gene links
Show Anatomy links
A neuronal isoform of CPEB regulates local protein synthesis and stabilizes synapse-specific long-term facilitation in aplysia.
Si K
,
Giustetto M
,
Etkin A
,
Hsu R
,
Janisiewicz AM
,
Miniaci MC
,
Kim JH
,
Zhu H
,
Kandel ER
.
???displayArticle.abstract???
Synapse-specific facilitation requires rapamycin-dependent local protein synthesis at the activated synapse. In Aplysia, rapamycin-dependent local protein synthesis serves two functions: (1) it provides a component of the mark at the activated synapse and thereby confers synapse specificity and (2) it stabilizes the synaptic growth associated with long-term facilitation. Here we report that a neuron-specific isoform of cytoplasmic polyadenylation element binding protein (CPEB) regulates this synaptic protein synthesis in an activity-dependent manner. Aplysia CPEB protein is upregulated locally at activated synapses, and it is needed not for the initiation but for the stable maintenance of long-term facilitation. We suggest that Aplysia CPEB is one of the stabilizing components of the synaptic mark.
Figure S1.
Alignment of the C-terminal domain of the Aplysia CPEB (Aplysia), DrosophilaCG5735RA (Drosophila), Human KIAA0940 (Human) and Xenopus laveisoocyte CPEB ( Xenopus). Two RNA binding motifs are marked as RRM1 and RRM2. The program ClustalV is used for alignment.
Figure S5.
(A) The cytoplasmic polyadenylation element (CPE) UUUUUUAU and hexanucleotide Poly A signal AAUAAA is underlined in the 3â² UTR of Aplysia neuronal actin mRNA.
(B) N-Actin 3â²UTR contain a functional CPE element. In vitro transcribed luciferase mRNA was injected (â¼100 ng) in stage VI Xenopus oocyte. For each mRNA, 20 oocytes were injected and randomly divided into four groups (5 oocytes/group). Two groups were stimulated with 10 μM progesterone for 8 hr and the luciferase activity of the stimulated and unstimulated samples were measured. The luciferase activity of the untreated sample is considered as one unit and the increase in luciferase activity is shown as fold induction. Data from two independent experiments (four samples for each data point) are used.
(C) 240 nucleotides from the 3â²UTR of N-actin mRNA with either wild-type CPE or mutated CPE element was transcribed with in presence of [Full-size image (<1 K)] UTP and mRNA cap analog. The Full-size image (<1 K)-labeled mRNA was injected in stage VI Xenopus oocyte and treated with 10 μM progesterone. At indicated time, total RNA was prepared, analyzed on 5% polyacrylamide gel, and autoradiographed. Increase in the poly A tail of the mRNA with wild-type CPE is indicated.
