Regulated proteolysis of APP and ApoE receptors.

Molecular Neurobiology
Hyang-Sook Hoe, G William Rebeck

Abstract

The beta-amyloid precursor protein (APP) shares intracellular and extracellular-binding partners with the family of receptors for apolipoprotein E (apoE). Binding of APP and apoE receptors to specific extracellular matrix proteins (F-spondin and Reelin) promotes their presence on the cell surface and influences whether they will interact with specific cytoplasmic adaptor proteins. Cleavage of APP and apoE receptors at the cell surface occurs by alpha-secretase activities; thus, the processing of these proteins can be regulated by their trafficking either to or from the cell surface. Their cleavages can also be regulated by tissue inhibitor of metalloproteinase-3 (TIMP-3), a metalloprotease inhibitor in the extracellular matrix. ApoE receptors have functions in neuronal migration during development and in proper synaptic function in the adult. Thus, the functions of apoE receptors and by analogy of APP will be modified by the various extracellular and intracellular interactions reviewed in this paper.

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Citations

Mar 17, 2009·Journal of Neuroimmune Pharmacology : the Official Journal of the Society on NeuroImmune Pharmacology·Cristian L AchimUNKNOWN Neurobehavioral Research Center
Feb 25, 2011·PloS One·Sonya B DumanisHyang-Sook Hoe
Jul 7, 2012·PloS One·Veronica AkleIrina V Zhdanova
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Jan 8, 2013·Behavioural Brain Research·Pierre-Henri MoreauChantal Mathis
Dec 2, 2008·Seminars in Cell & Developmental Biology·Maria-Paz Marzolo, Guojun Bu
Mar 17, 2017·Frontiers in Molecular Neuroscience·Theresa PohlkampJoachim Herz
Apr 24, 2014·The Journal of Biological Chemistry·Shailaja D DivekarG William Rebeck
Jul 26, 2016·Frontiers in Cellular Neuroscience·Hans H Bock, Petra May
Feb 25, 2017·Intrinsically Disordered Proteins·Oluwole AlowoloduVladimir N Uversky

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