The Alzheimer Amyloid Precursor Protein (APP) and FE65, an APP-binding Protein, Regulate Cell Movement

doi:10.1083/jcb.153.7.1403

Published online 18 June 2001. doi:10.1083/jcb.153.7.1403

This Article

	Full Text
	Full Text (PDF, 1036K)
	PPT slides of all figures
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Sabo, S. L.
	Articles by Greengard, P.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Sabo, S. L.
	Articles by Greengard, P.


Social Bookmarking

	What's this?

© The Rockefeller University Press, 0021-9525/2001/6/1403/ $5.00
The Journal of Cell Biology, Volume 153, Number 7, June 25, 2001 1403-1414

Original Article

The Alzheimer Amyloid Precursor Protein (APP) and FE65, an APP-binding Protein, Regulate Cell Movement

Shasta L. Sabo^a, Annat F. Ikin^a,b, Joseph D. Buxbaum^a,b, and Paul Greengard^a
^a Laboratory of Molecular and Cellular Neuroscience and the Zachary and Elizabeth M. Fisher Center, The Rockefeller University, New York, New York 10021
^b Laboratory of Molecular Neuropsychiatry, Departments of Psychiatry and Neurobiology, Mount Sinai School of Medicine, New York, New York 10029

Correspondence to: Shasta L. Sabo, Center for Neuroscience, University of California at Davis, 1544 Newton Ct., Davis, CA 95616. Tel:(530) 754-6990 Fax:(530) 757-8827 E-mail:slsabo{at}ucdavis.edu.

FE65 binds to the Alzheimer amyloid precursor protein (APP),but the function of this interaction has not been identified.Here, we report that APP and FE65 are involved in regulationof cell movement. APP and FE65 colocalize with actin and Mena,an Abl-associated signaling protein thought to regulate actindynamics, in lamellipodia. APP and FE65 specifically concentratewith ß1-integrin in dynamic adhesion sites known asfocal complexes, but not in more static adhesion sites knownas focal adhesions. Overexpression of APP accelerates cell migrationin an MDCK cell wound–healing assay. Coexpression of APPand FE65 dramatically enhances the effect of APP on cell movement,probably by regulating the amount of APP at the cell surface.These data are consistent with a role for FE65 and APP, possiblyin a Mena-containing macromolecular complex, in regulation ofactin-based motility.

Key Words: amyloid precursor protein, FE65, Mena, cell movement, adhesion

Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Add to Reddit Reddit Add to Technorati Technorati What's this?

This article has been cited by other articles:

Stante, M., Minopoli, G., Passaro, F., Raia, M., Vecchio, L. D., Russo, T. (2009). Fe65 is required for Tip60-directed histone H4 acetylation at DNA strand breaks. Proc. Natl. Acad. Sci. USA 106: 5093-5098 [Abstract] [Full Text]
Muresan, V., Varvel, N. H., Lamb, B. T., Muresan, Z. (2009). The Cleavage Products of Amyloid-{beta} Precursor Protein Are Sorted to Distinct Carrier Vesicles That Are Independently Transported within Neurites. J. Neurosci. 29: 3565-3578 [Abstract] [Full Text]
Takayama, K.-i., Tsutsumi, S., Suzuki, T., Horie-Inoue, K., Ikeda, K., Kaneshiro, K., Fujimura, T., Kumagai, J., Urano, T., Sakaki, Y., Shirahige, K., Sasano, H., Takahashi, S., Kitamura, T., Ouchi, Y., Aburatani, H., Inoue, S. (2009). Amyloid Precursor Protein Is a Primary Androgen Target Gene That Promotes Prostate Cancer Growth. Cancer Res. 69: 137-142 [Abstract] [Full Text]
Radzimanowski, J., Ravaud, S., Schlesinger, S., Koch, J., Beyreuther, K., Sinning, I., Wild, K. (2008). Crystal Structure of the Human Fe65-PTB1 Domain. J. Biol. Chem. 283: 23113-23120 [Abstract] [Full Text]
Arvidsson, Y., Andersson, E., Bergstrom, A., Andersson, M. K, Altiparmak, G., Illerskog, A.-C., Ahlman, H., Lamazhapova, D., Nilsson, O. (2008). Amyloid precursor-like protein 1 is differentially upregulated in neuroendocrine tumours of the gastrointestinal tract. Endocr Relat Cancer 15: 569-581 [Abstract] [Full Text]
Young-Pearse, T. L., Bai, J., Chang, R., Zheng, J. B., LoTurco, J. J., Selkoe, D. J. (2007). A Critical Function for -Amyloid Precursor Protein in Neuronal Migration Revealed by In Utero RNA Interference. J. Neurosci. 27: 14459-14469 [Abstract] [Full Text]
Wolfe, M. S., Guenette, S. Y. (2007). APP at a glance. J. Cell Sci. 120: 3157-3161 [Full Text]
Kraemer, B. C., Schellenberg, G. D. (2007). SUT-1 enables tau-induced neurotoxicity in C. elegans. Hum Mol Genet 16: 1959-1971 [Abstract] [Full Text]
Bao, J., Cao, C., Zhang, X., Jiang, F., Nicosia, S. V., Bai, W. (2007). Suppression of {beta}-Amyloid Precursor Protein Signaling into the Nucleus by Estrogens Mediated through Complex Formation between the Estrogen Receptor and Fe65. Mol. Cell. Biol. 27: 1321-1333 [Abstract] [Full Text]
Minopoli, G., Stante, M., Napolitano, F., Telese, F., Aloia, L., De Felice, M., Di Lauro, R., Pacelli, R., Brunetti, A., Zambrano, N., Russo, T. (2007). Essential Roles for Fe65, Alzheimer Amyloid Precursor-binding Protein, in the Cellular Response to DNA Damage. J. Biol. Chem. 282: 831-835 [Abstract] [Full Text]
Gomes, R. A., Hampton, C., El-Sabeawy, F., Sabo, S. L., McAllister, A. K. (2006). The Dynamic Distribution of TrkB Receptors before, during, and after Synapse Formation between Cortical Neurons.. J. Neurosci. 26: 11487-11500 [Abstract] [Full Text]
Hoe, H.-S., Magill, L. A., Guenette, S., Fu, Z., Vicini, S., Rebeck, G. W. (2006). FE65 Interaction with the ApoE Receptor ApoEr2. J. Biol. Chem. 281: 24521-24530 [Abstract] [Full Text]
Heredia, L., Helguera, P., de Olmos, S., Kedikian, G., Sola Vigo, F., LaFerla, F., Staufenbiel, M., de Olmos, J., Busciglio, J., Caceres, A., Lorenzo, A. (2006). Phosphorylation of actin-depolymerizing factor/cofilin by LIM-kinase mediates amyloid beta-induced degeneration: a potential mechanism of neuronal dystrophy in Alzheimer's disease.. J. Neurosci. 26: 6533-6542 [Abstract] [Full Text]
Neumann, S., Schobel, S., Jager, S., Trautwein, A., Haass, C., Pietrzik, C. U., Lichtenthaler, S. F. (2006). Amyloid Precursor-like Protein 1 Influences Endocytosis and Proteolytic Processing of the Amyloid Precursor Protein. J. Biol. Chem. 281: 7583-7594 [Abstract] [Full Text]
Masin, M., Kerschensteiner, D., Dumke, K., Rubio, M. E., Soto, F. (2006). Fe65 Interacts with P2X2 Subunits at Excitatory Synapses and Modulates Receptor Function. J. Biol. Chem. 281: 4100-4108 [Abstract] [Full Text]
Yang, Z., Cool, B. H., Martin, G. M., Hu, Q. (2006). A Dominant Role for FE65 (APBB1) in Nuclear Signaling. J. Biol. Chem. 281: 4207-4214 [Abstract] [Full Text]
Ryan, K. A., Pimplikar, S. W. (2005). Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain. JCB 171: 327-335 [Abstract] [Full Text]
Hu, Q., Wang, L., Yang, Z., Cool, B. H., Zitnik, G., Martin, G. M. (2005). Endoproteolytic Cleavage of FE65 Converts the Adaptor Protein to a Potent Suppressor of the sAPP{alpha} Pathway in Primates. J. Biol. Chem. 280: 12548-12558 [Abstract] [Full Text]
Roux, K. J., Amici, S. A., Fletcher, B. S., Notterpek, L. (2005). Modulation of Epithelial Morphology, Monolayer Permeability, and Cell Migration by Growth Arrest Specific 3/Peripheral Myelin Protein 22. Mol. Biol. Cell 16: 1142-1151 [Abstract] [Full Text]
Kato, Y., Nagata, K., Takahashi, M., Lian, L., Herrero, J. J., Sudol, M., Tanokura, M. (2004). Common Mechanism of Ligand Recognition by Group II/III WW Domains: REDEFINING THEIR FUNCTIONAL CLASSIFICATION. J. Biol. Chem. 279: 31833-31841 [Abstract] [Full Text]
Cao, X., Sudhof, T. C. (2004). Dissection of Amyloid-{beta} Precursor Protein-dependent Transcriptional Transactivation. J. Biol. Chem. 279: 24601-24611 [Abstract] [Full Text]
Taru, H., Suzuki, T. (2004). Facilitation of Stress-induced Phosphorylation of {beta}-Amyloid Precursor Protein Family Members by X11-like/Mint2 Protein. J. Biol. Chem. 279: 21628-21636 [Abstract] [Full Text]
Frame, M. C. (2004). Newest findings on the oldest oncogene; how activated src does it. J. Cell Sci. 117: 989-998 [Abstract] [Full Text]
Muresan, Z., Muresan, V. (2004). A phosphorylated, carboxy-terminal fragment of {beta}-amyloid precursor protein localizes to the splicing factor compartment. Hum Mol Genet 13: 475-488 [Abstract] [Full Text]
Hansel, D. E., Rahman, A., Wehner, S., Herzog, V., Yeo, C. J., Maitra, A. (2003). Increased Expression and Processing of the Alzheimer Amyloid Precursor Protein in Pancreatic Cancer May Influence Cellular Proliferation. Cancer Res. 63: 7032-7037 [Abstract] [Full Text]
Sabo, S. L., Ikin, A. F., Buxbaum, J. D., Greengard, P. (2003). The Amyloid Precursor Protein and Its Regulatory Protein, FE65, in Growth Cones and Synapses In Vitro and In Vivo. J. Neurosci. 23: 5407-5415 [Abstract] [Full Text]
Gassen, G. V., Annaert, W. (2003). Amyloid, Presenilins, and Alzheimer's Disease. Neuroscientist 9: 117-126 [Abstract]
Rappoport, J. Z., Simon, S. M. (2003). Real-time analysis of clathrin-mediated endocytosis during cell migration. J. Cell Sci. 116: 847-855 [Abstract] [Full Text]
Grace, E. A., Busciglio, J. (2003). Aberrant Activation of Focal Adhesion Proteins Mediates Fibrillar Amyloid beta -Induced Neuronal Dystrophy. J. Neurosci. 23: 493-502 [Abstract] [Full Text]
Russo, C., Dolcini, V., Salis, S., Venezia, V., Zambrano, N., Russo, T., Schettini, G. (2002). Signal Transduction through Tyrosine-phosphorylated C-terminal Fragments of Amyloid Precursor Protein via an Enhanced Interaction with Shc/Grb2 Adaptor Proteins in Reactive Astrocytes of Alzheimer's Disease Brain. J. Biol. Chem. 277: 35282-35288 [Abstract] [Full Text]
Bruni, P., Minopoli, G., Brancaccio, T., Napolitano, M., Faraonio, R., Zambrano, N., Hansen, U., Russo, T. (2002). Fe65, a Ligand of the Alzheimer's beta -Amyloid Precursor Protein, Blocks Cell Cycle Progression by Down-regulating Thymidylate Synthase Expression. J. Biol. Chem. 277: 35481-35488 [Abstract] [Full Text]
Suh, Y.-H., Checler, F. (2002). Amyloid Precursor Protein, Presenilins, and alpha -Synuclein: Molecular Pathogenesis and Pharmacological Applications in Alzheimer's Disease. Pharmacol. Rev. 54: 469-525 [Abstract] [Full Text]
Loureiro, J. J., Rubinson, D. A., Bear, J. E., Baltus, G. A., Kwiatkowski, A. V., Gertler, F. B. (2002). Critical Roles of Phosphorylation and Actin Binding Motifs, but Not the Central Proline-rich Region, for Ena/Vasodilator-stimulated Phosphoprotein (VASP) Function during Cell Migration. Mol. Biol. Cell 13: 2533-2546 [Abstract] [Full Text]
Brooks, A. I., Stein, C. S., Hughes, S. M., Heth, J., McCray, P. M. Jr., Sauter, S. L., Johnston, J. C., Cory-Slechta, D. A., Federoff, H. J., Davidson, B. L. (2002). From the Cover: Functional correction of established central nervous system deficits in an animal model of lysosomal storage disease with feline immunodeficiency virus-based vectors. Proc. Natl. Acad. Sci. USA 99: 6216-6221 [Abstract] [Full Text]
Hu, Q., Cool, B. H., Wang, B., Hearn, M. G., Martin, G. M. (2002). A candidate molecular mechanism for the association of an intronic polymorphism of FE65 with resistance to very late onset dementia of the Alzheimer type. Hum Mol Genet 11: 465-475 [Abstract] [Full Text]
Zambrano, N., Bimonte, M., Arbucci, S., Gianni, D., Russo, T., Bazzicalupo, P. (2002). feh-1 and apl-1, the Caenorhabditis elegans orthologues of mammalian Fe65 and {beta}-amyloid precursor protein genes, are involved in the same pathway that controls nematode pharyngeal pumping. J. Cell Sci. 115: 1411-1422 [Abstract] [Full Text]
Gao, Y., Pimplikar, S. W. (2001). The gamma -secretase-cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus. Proc. Natl. Acad. Sci. USA 10.1073/pnas.261463298v1 [Abstract] [Full Text]
Brooks, A. I., Stein, C. S., Hughes, S. M., Heth, J., McCray, P. M. Jr., Sauter, S. L., Johnston, J. C., Cory-Slechta, D. A., Federoff, H. J., Davidson, B. L. (2002). From the Cover: Functional correction of established central nervous system deficits in an animal model of lysosomal storage disease with feline immunodeficiency virus-based vectors. Proc. Natl. Acad. Sci. USA 99: 6216-6221 [Abstract] [Full Text]
Gao, Y., Pimplikar, S. W. (2001). The gamma -secretase-cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus. Proc. Natl. Acad. Sci. USA 98: 14979-14984 [Abstract] [Full Text]