Title
Amyloid precursor proteins anchor CPEB to membranes and promote polyadenylation-induced translation
GSBS Program
Biochemistry & Molecular Pharmacology
UMMS Affiliation
Graduate School of Biomedical Sciences; Program in Molecular Medicine
Date
11-30-2005
Document Type
Article
Medical Subject Headings
Amyloid beta-Protein Precursor; Animals; Cell Membrane; Cytoplasm; Gene Library; Mice; Neurons; Phosphorylation; *Polyadenylation; *Protein Biosynthesis; Protein-Serine-Threonine Kinases; RNA, Messenger; RNA-Binding Proteins; Serine; Two-Hybrid System Techniques
Disciplines
Life Sciences | Medicine and Health Sciences
Abstract
The cytoplasmic polyadenylation element (CPE) binding factor, CPEB, is a sequence-specific RNA binding protein that controls polyadenylation-induced translation in germ cells and at postsynaptic sites of neurons. A yeast two-hybrid screen with a mouse brain cDNA library identified the transmembrane amyloid precursor-like protein 1 (APLP1) as a CPEB-interacting factor. CPEB binds the small intracellular domain (ICD) of APLP1 and the related proteins APLP2 and APP. These proteins promote polyadenylation and translation by stimulating Aurora A catalyzed CPEB serine 174 phosphorylation. Surprisingly, CPEB, Maskin, CPSF, and several other factors involved in polyadenylation and translation and CPE-containing RNA are all detected on membranes by cell fractionation and immunoelectron microscopy. Moreover, most of the RNA that undergoes polyadenylation does so in membrane-containing fractions. These data demonstrate a link between cytoplasmic polyadenylation and membrane association and implicate APP family member proteins as anchors for localized mRNA polyadenylation and translation.
Rights and Permissions
Citation: Mol Cell Biol. 2005 Dec;25(24):10930-9. Link to article on publisher's site