Abstract
Eukaryotic cells express numerous ArfGAPs (ADP-ribosylation factor GTPase-activating proteins). There is increasing knowledge about the function of the brain-specific protein ADAP1 [ArfGAP with dual pleckstrin homology (PH) domain] as well as about its biochemical properties. The ADAP subfamily, also designated centaurin-α, has an N-terminal ArfGAP domain followed by two PH domains. The mammalian ADAP subfamily consists of two identified isoforms, ADAP1 and ADAP2 (centaurin-α1 and -α2). ADAP1 is highly expressed in neurons. We highlight the functional roles of ADAP1 in neuronal differentiation and neurodegeneration. Because of interactions with different proteins and phosphoinositol-lipids, ADAP1 can function as a scaffolding protein in several signal transduction pathways. Firstly, ADAP1 mediates cytoskeletal crosstalk. This is indicated by multiple interactions of ADAP1 with components of the actin and microtubule cytoskeleton. Secondly, regulation of neuronal polarity formation and axon specification by ADAP1 is suggested by crystal structural data obtained for human ADAP1, and the complexes of ADAP1-Ins(1,3,4,5)P4 and/or the forkhead-associated domain of the kinesin KIF13B. These structures support the concept that a KIF13B-ADAP1 complex enhances the local accumulation of PtdIns(3,4,5)P3 at the tips of neurites, and thus favors neuronal polarity. Thirdly, recent evidence unravels a pathological role of ADAP1 because upregulation of ADAP1 by amyloid β-peptide causes ADAP1-Ras-ERK-dependent translocation of Elk-1 to mitochondria. This impairs mitochondrial functions with subsequent synaptic dysfunction and exacerbates neurodegeneration, as in Alzheimer’s disease.
About the authors
Rolf Stricker studied Biochemistry at the University of Tübingen, and graduated in 1992. In 1996 he received his PhD in Biochemistry at the Institute of Physiological Chemistry of the University of Tübingen. From 1994 to March 2014 he worked at the Institute of Neurobiochemistry of the Otto-von-Guericke University, Magdeburg as postdoctoral fellow. Since April 2014 he is a member of the Institute for Biochemistry and Cell Biology of the Otto-von-Guericke University, Magdeburg.
Georg Reiser did his PhD at the Max-Planck Institute of Biochemistry in Martinsried and the Ludwig-Maximilians University in Munich under the supervision of B. Hamprecht in the department of F. Lynen. After working as research fellow in the Institute for Physiological Chemistry in Wurzburg, he obtained a DFG-fellowship with further training in electrophysiology at the University College London, Department of Biophysics under R. Miledi. There, he studied nicotinic acetylcholine receptor ion channels. From 1984 he continued research in mechanisms of neural molecular signaling, focusing on calcium regulation and identification of the inositol(1,3,4,5)P4 receptor protein, designated p42IP4. From 1994 he is professor for biochemistry and neurochemistry in Magdeburg, Medical Faculty with research on molecular mechanisms of neuroprotection in ischemia and stroke, covering functions of mitochondria, protease-activated receptors, P2Y nucleotide receptors, nuclear Peroxisome Proliferators Activated Receptors, and iPLA2 isoforms in neurodegenerative diseases.
Acknowledgments
The work in the authors’ laboratory has been supported by grants from BMBF, DFG, and Land Sachsen-Anhalt. The contributing author especially thanks to all his collaborators, who made substantial efforts to elucidate over the years the properties and functions of ADAP1 (p42IP4), Frédéric Donié, Eckehard Hülser, Ute Kunzelmann, Michael Aggensteiner, Fariba Sedehizade, Andrea Haase, and Theo Hanck.
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