QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

HOME  |   SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

This Article Full Text Full Text (PDF) Submit an eLetter Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (24) Citing Articles via Google Scholar Google Scholar Articles by Torroja, L. Articles by White, K. Search for Related Content PubMed PubMed Citation Articles by Torroja, L. Articles by White, K.

 Previous Article  |  Next Article 

Volume 16, Number 15, Issue of August 1, 1996 pp. 4638-4650
Copyright ©1996 Society for Neuroscience

APPL, the Drosophila Member of the APP-Family, Exhibits Differential Trafficking and Processing in CNS Neurons

Received April 4, 1996; revised May 1, 1996; accepted May 7, 1996.

Laura Torroja, Liqun Luo, and Kalpana White

Department of Biology and Volen National Center for Complex Systems, Brandeis University, Waltham, Massachusetts 02254

The Drosophila Appl gene encodes a transmembrane protein that is expressed exclusively in neurons. Amino acid comparisons show that APPL protein is a member of the amyloid precursor protein (APP)-like family of proteins. Similar to mammalian APP-family proteins, APPL is synthesized as a transmembrane holoprotein and cleaved to release a large secreted amino-terminal domain. Using immunocytochemical methods, we have analyzed the distribution of APPL in the Drosophila CNS. Surprisingly, although APPL is present in all neuronal cell bodies, the neuropil shows stereotypic differential distribution. Double-labeling experiments with different neuronal markers were used to distinguish between APPL associated with neuronal processes or extracellular matrix. The distribution of APPL protein produced from transgenes encoding wild-type (APPL), secretion-defective (APPL^sd), and constitutively secreted (APPL^s) forms was analyzed in an Appl-deficient background to determine which APPL form is associated with different neuropil regions. We found that APPL^sd protein is enriched where APPL immunoreactivity coincides with neuronal processes. In contrast, APPL^s preferentially localizes to those parts of the neuropil that show a diffuse APPL signal that rarely colocalizes with processes, and thus seems to be a component of the extracellular matrix. These data indicate that proteolytic cleavage and trafficking of APPL is differentially regulated in different neuronal populations. Through metamorphosis, APPL is especially abundant in growing axons and in areas where synapses are forming. Interestingly, in adult brains, APPL protein is enriched in the mushroom bodies and to a lesser extent in the central complex, structures involved in learning and memory.

Key words: amyloid precursor protein family; neuropil distribution; mushroom bodies; protein sorting and processing; mutant transgenes; Alzheimer's disease

This article has been cited by other articles:

				J. Ashley, M. Packard, B. Ataman, and V. Budnik Fasciclin II Signals New Synapse Formation through Amyloid Precursor Protein and the Scaffolding Protein dX11/Mint J. Neurosci., June 22, 2005; 25(25): 5943 - 5955. [Abstract] [Full Text] [PDF]

				W. T. Kimberly, J. B. Zheng, T. Town, R. A. Flavell, and D. J. Selkoe Physiological Regulation of the {beta}-Amyloid Precursor Protein Signaling Domain by c-Jun N-Terminal Kinase JNK3 during Neuronal Differentiation J. Neurosci., June 8, 2005; 25(23): 5533 - 5543. [Abstract] [Full Text] [PDF]

				N. Kotani, S. Kitazume, K. Kamimura, S. Takeo, T. Aigaki, H. Nakato, and Y. Hashimoto Characterization of Drosophila Aspartic Proteases That Induce the Secretion of a Golgi-Resident Transferase, Heparan Sulfate 6-O-Sulfotransferase J. Biochem., March 1, 2005; 137(3): 315 - 322. [Abstract] [Full Text] [PDF]

				K. D. Finley, P. T. Edeen, R. C. Cumming, M. D. Mardahl-Dumesnil, B. J. Taylor, M. H. Rodriguez, C. E. Hwang, M. Benedetti, and M. McKeown blue cheese Mutations Define a Novel, Conserved Gene Involved in Progressive Neural Degeneration J. Neurosci., February 15, 2003; 23(4): 1254 - 1264. [Abstract] [Full Text] [PDF]

				H. Taru, K.-i. Iijima, M. Hase, Y. Kirino, Y. Yagi, and T. Suzuki Interaction of Alzheimer's beta -Amyloid Precursor Family Proteins with Scaffold Proteins of the JNK Signaling Cascade J. Biol. Chem., May 24, 2002; 277(22): 20070 - 20078. [Abstract] [Full Text] [PDF]

				A. R. White, G. Multhaup, D. Galatis, W. J. McKinstry, M. W. Parker, R. Pipkorn, K. Beyreuther, C. L. Masters, and R. Cappai Contrasting, Species-Dependent Modulation of Copper-Mediated Neurotoxicity by the Alzheimer's Disease Amyloid Precursor Protein J. Neurosci., January 15, 2002; 22(2): 365 - 376. [Abstract] [Full Text] [PDF]

				L. Torroja, M. Packard, M. Gorczyca, K. White, and V. Budnik The Drosophila beta -Amyloid Precursor Protein Homolog Promotes Synapse Differentiation at the Neuromuscular Junction J. Neurosci., September 15, 1999; 19(18): 7793 - 7803. [Abstract] [Full Text] [PDF]

				X. Xu, D. Yang, T. Wyss-Coray, J. Yan, L. Gan, Y. Sun, and L. Mucke Wild-type but not Alzheimer-mutant amyloid precursor protein confers resistance against p53-mediated apoptosis PNAS, June 22, 1999; 96(13): 7547 - 7552. [Abstract] [Full Text] [PDF]

				E. Masliah, J. Raber, M. Alford, M. Mallory, M. P. Mattson, D. Yang, D. Wong, and L. Mucke Amyloid Protein Precursor Stimulates Excitatory Amino Acid Transport. IMPLICATIONS FOR ROLES IN NEUROPROTECTION AND PATHOGENESIS J. Biol. Chem., May 15, 1998; 273(20): 12548 - 12554. [Abstract] [Full Text] [PDF]

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help