JBC Focus on PI3-Kinase with Echelon

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M000389200 on March 16, 2000

J. Biol. Chem., Vol. 275, Issue 21, 15733-15740, May 26, 2000
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
275/21/15733    most recent
M000389200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Maas, T.
Right arrow Articles by Brandt, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Maas, T.
Right arrow Articles by Brandt, R.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Interaction of Tau with the Neural Membrane Cortex Is Regulated by Phosphorylation at Sites That Are Modified in Paired Helical Filaments*

Thorsten Maas, Jochen Eidenmüller, and Roland BrandtDagger

From the Department of Neurobiology, Interdisziplinäres Zentrum für Neurowissenschaften (IZN), University of Heidelberg, Im Neuenheimer Feld 364, D-69120 Heidelberg, Germany

The axonal microtubule-associated phosphoprotein tau interacts with neural plasma membrane (PM) components during neuronal development (Brandt, R., Léger, J., and Lee, G. (1995) J. Cell Biol. 131, 1327-1340). To analyze the mechanism and potential regulation of tau's PM association, a method was developed to isolate PM-associated tau using microsphere separation of surface-biotinylated cells. We show that tau's PM association requires an intact membrane cortex and that PM-associated tau and cytosolic tau are differentially phosphorylated at sites detected by several Alzheimer's disease (AD) diagnostic antibodies (Ser199/Ser202, Thr231, and Ser396/Ser404). In polar neurons, the association of endogenous tau phosphoisoforms with the membrane cortex correlates with an enrichment in the axonal compartment. To test for a direct effect of AD-specific tau modifications in determining tau's interactions, a phosphomutant that simulates an AD-like hyperphosphorylation of tau was produced by site-directed mutagenesis of Ser/Thr residues to negatively charged amino acids (Glu). These mutations completely abolish tau's association with the membrane cortex; however, the construct retains its capability to bind to microtubules. The data suggest that a loss of tau's association with the membrane cortex as a result of phosphorylation at sites that are modified during disease contributes to somatodendritic tau accumulation, axonal microtubule disintegration, and neuronal death characteristic for AD.

* This work was supported in part by the Deutsche Forschungsgemeinschaft (SFB 317, Teilprojekt D3), and the "Landesforschungsschwerpunkt Protein-Faltung und Transport" (to R. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Recipient of a Heisenberg fellowship from the Deutsche Forschungsgemeinschaft. To whom correspondence should be addressed. Tel.: 49-6221-548329; Fax: 49-6221-544496; E-mail: Brandt@sun0.urz.uni-heidelberg.de.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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:


Home page
 J. Neurosci.Home page
E. Planel, P. Krishnamurthy, T. Miyasaka, L. Liu, M. Herman, A. Kumar, A. Bretteville, H. Y. Figueroa, W. Haung Yu, R. A. Whittington, et al.
Anesthesia-Induced Hyperphosphorylation Detaches 3-Repeat Tau from Microtubules without Affecting Their Stability In Vivo
J. Neurosci., November 26, 2008; 28(48): 12798 - 12807.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. H. Reynolds, C. J. Garwood, S. Wray, C. Price, S. Kellie, T. Perera, M. Zvelebil, A. Yang, P. W. Sheppard, I. M. Varndell, et al.
Phosphorylation Regulates Tau Interactions with Src Homology 3 Domains of Phosphatidylinositol 3-Kinase, Phospholipase C{gamma}1, Grb2, and Src Family Kinases
J. Biol. Chem., June 27, 2008; 283(26): 18177 - 18186.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
E. Planel, Y. Tatebayashi, T. Miyasaka, L. Liu, L. Wang, M. Herman, W. H. Yu, J. A. Luchsinger, B. Wadzinski, K. E. Duff, et al.
Insulin Dysfunction Induces In Vivo Tau Hyperphosphorylation through Distinct Mechanisms
J. Neurosci., December 12, 2007; 27(50): 13635 - 13648.
[Abstract] [Full Text] [PDF]

Home page
 FASEB J.Home page
J.-Z. Yu and M. M. Rasenick
Tau associates with actin in differentiating PC12 cells
FASEB J, July 1, 2006; 20(9): 1452 - 1461.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
N. Shahani, S. Subramaniam, T. Wolf, C. Tackenberg, and R. Brandt
Tau aggregation and progressive neuronal degeneration in the absence of changes in spine density and morphology after targeted expression of Alzheimer's disease-relevant tau constructs in organotypic hippocampal slices.
J. Neurosci., May 31, 2006; 26(22): 6103 - 6114.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Mi, P. J. Dolan, and G. V. W. Johnson
The Low Density Lipoprotein Receptor-related Protein 6 Interacts with Glycogen Synthase Kinase 3 and Attenuates Activity
J. Biol. Chem., February 24, 2006; 281(8): 4787 - 4794.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
P. Derkinderen, T. M. E. Scales, D. P. Hanger, K.-Y. Leung, H. L. Byers, M. A. Ward, C. Lenz, C. Price, I. N. Bird, T. Perera, et al.
Tyrosine 394 Is Phosphorylated in Alzheimer's Paired Helical Filament Tau and in Fetal Tau with c-Abl as the Candidate Tyrosine Kinase
J. Neurosci., July 13, 2005; 25(28): 6584 - 6593.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
T. Kawarabayashi, M. Shoji, L. H. Younkin, L. Wen-Lang, D. W. Dickson, T. Murakami, E. Matsubara, K. Abe, K. H. Ashe, and S. G. Younkin
Dimeric Amyloid {beta} Protein Rapidly Accumulates in Lipid Rafts followed by Apolipoprotein E and Phosphorylated Tau Accumulation in the Tg2576 Mouse Model of Alzheimer's Disease
J. Neurosci., April 14, 2004; 24(15): 3801 - 3809.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Milakovic, J. Tucholski, E. McCoy, and G. V. W. Johnson
Intracellular Localization and Activity State of Tissue Transglutaminase Differentially Impacts Cell Death
J. Biol. Chem., March 5, 2004; 279(10): 8715 - 8722.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. Piontek and R. Brandt
Differential and Regulated Binding of cAMP-dependent Protein Kinase and Protein Kinase C Isoenzymes to Gravin in Human Model Neurons: EVIDENCE THAT GRAVIN PROVIDES A DYNAMIC PLATFORM FOR THE LOCALIZATION OF KINASES DURING NEURONAL DEVELOPMENT
J. Biol. Chem., October 3, 2003; 278(40): 38970 - 38979.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H.-Y. Wang, W. Li, N. J. Benedetti, and D. H. S. Lee
{alpha}7 Nicotinic Acetylcholine Receptors Mediate {beta}-Amyloid Peptide-induced Tau Protein Phosphorylation
J. Biol. Chem., August 22, 2003; 278(34): 31547 - 31553.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J.-H. Cho and G. V. W. Johnson
Glycogen Synthase Kinase 3beta Phosphorylates Tau at Both Primed and Unprimed Sites. DIFFERENTIAL IMPACT ON MICROTUBULE BINDING
J. Biol. Chem., January 3, 2003; 278(1): 187 - 193.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
T. Fath, J. Eidenmuller, and R. Brandt
Tau-Mediated Cytotoxicity in a Pseudohyperphosphorylation Model of Alzheimer's Disease
J. Neurosci., November 15, 2002; 22(22): 9733 - 9741.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
M. A. Utton, J. Connell, A. A. Asuni, M. van Slegtenhorst, M. Hutton, R. de Silva, A. J. Lees, C. C. J. Miller, and B. H. Anderton
The Slow Axonal Transport of the Microtubule-Associated Protein Tau and the Transport Rates of Different Isoforms and Mutants in Cultured Neurons
J. Neurosci., August 1, 2002; 22(15): 6394 - 6400.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
C. Klein, E.-M. Kramer, A.-M. Cardine, B. Schraven, R. Brandt, and J. Trotter
Process Outgrowth of Oligodendrocytes Is Promoted by Interaction of Fyn Kinase with the Cytoskeletal Protein Tau
J. Neurosci., February 1, 2002; 22(3): 698 - 707.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.