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The cytosolic domain of APP induces the relocalization of dynamin 3 in hippocampal neurons
Author(s) -
Meckler X.,
Bertandeau E.,
McNiven M. A.,
Allinquant B.,
Hémar A.
Publication year - 2006
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1111/j.1460-9568.2006.05141.x
Subject(s) - neurite , dynamin , hippocampal formation , gtpase , cytosol , microbiology and biotechnology , amyloid precursor protein , neuroscience , intracellular , chemistry , biology , biochemistry , cell , endocytosis , alzheimer's disease , pathology , medicine , in vitro , disease , enzyme
Amyloid precursor protein (APP) has been the subject of intense research to uncover its implication in Alzheimer's disease. Its physiological function is, however, still poorly understood. Herein, we investigated its possible influence on the development of cultured hippocampal neurons. A peptide corresponding to the APP intracellular domain linked to a cell‐penetrating peptide was used to alter the interactions of APP with its cytosolic partners. This treatment promoted the concentration of the cytosolic GTPase dynamin 3 (Dyn3) in neurite segments when most untreated cells displayed a homogenous punctate distribution of Dyn3. The Dyn3‐labelled segments were excluded from those revealed by APP staining after aldehyde fixation. Interestingly, after aldehyde fixation MAP2 also labelled segments excluded from APP‐stained segments. Thus APP is also a marker for the spacing pattern of neurites demonstrated by Taylor & Fallon (2006) J. Neurosci ., 26 , 1154–4463.