Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article Full Text Full Text (PDF, 2021K) PPT slides of all figures Supplemental Material Index 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 Goodchild, R. E. Articles by Dauer, W. T. Search for Related Content PubMed PubMed Citation Articles by Goodchild, R. E. Articles by Dauer, W. T. Related Collections Related Article Social Bookmarking                            What's this?

The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein

¹ Department of Neurology, Columbia University, New York, NY 10032
² Department of Pharmacology, Columbia University, New York, NY 10032

Correspondence to William Dauer: wtd3{at}columbia.edu

Abstract

A glutamic acid deletion (E) in the AAA+ protein torsinA causes DYT1 dystonia. Although the majority of torsinA resides within the endoplasmic reticulum (ER), torsinA binds a substrate in the lumen of the nuclear envelope (NE), and the E mutation enhances this interaction. Using a novel cell-based screen, we identify lamina-associated polypeptide 1 (LAP1) as a torsinA-interacting protein. LAP1 may be a torsinA substrate, as expression of the isolated lumenal domain of LAP1 inhibits the NE localization of "substrate trap" EQ-torsinA and EQ-torsinA coimmunoprecipitates with LAP1 to a greater extent than wild-type torsinA. Furthermore, we identify a novel transmembrane protein, lumenal domain like LAP1 (LULL1), which also appears to interact with torsinA. Interestingly, LULL1 resides in the main ER. Consequently, torsinA interacts directly or indirectly with a novel class of transmembrane proteins that are localized in different subdomains of the ER system, either or both of which may play a role in the pathogenesis of DYT1 dystonia.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Facebook    Reddit    Technorati    Twitter    What's this?

Related Article

Sticking to the nuclear envelope

Rabiya S. Tuma
J. Cell Biol. 2005 168: 848. [Full Text] [PDF]

This article has been cited by other articles:

• Naismith, T. V., Dalal, S., Hanson, P. I. (2009). Interaction of TorsinA with Its Major Binding Partners Is Impaired by the Dystonia-associated {Delta}GAG Deletion. J. Biol. Chem. 284: 27866-27874 [Abstract] [Full Text]  
• Martella, G., Tassone, A., Sciamanna, G., Platania, P., Cuomo, D., Viscomi, M. T., Bonsi, P., Cacci, E., Biagioni, S., Usiello, A., Bernardi, G., Sharma, N., Standaert, D. G., Pisani, A. (2009). Impairment of bidirectional synaptic plasticity in the striatum of a mouse model of DYT1 dystonia: role of endogenous acetylcholine. Brain 132: 2336-2349 [Abstract] [Full Text]  
• Giles, L. M., Li, L., Chin, L.-S. (2009). Printor, a Novel TorsinA-interacting Protein Implicated in Dystonia Pathogenesis. J. Biol. Chem. 284: 21765-21775 [Abstract] [Full Text]  
• Muller, U. (2009). The monogenic primary dystonias. Brain 132: 2005-2025 [Abstract] [Full Text]  
• Vander Heyden, A. B., Naismith, T. V., Snapp, E. L., Hodzic, D., Hanson, P. I. (2009). LULL1 Retargets TorsinA to the Nuclear Envelope Revealing an Activity That Is Impaired by the DYT1 Dystonia Mutation. Mol. Biol. Cell 20: 2661-2672 [Abstract] [Full Text]  
• Nery, F. C., Zeng, J., Niland, B. P., Hewett, J., Farley, J., Irimia, D., Li, Y., Wiche, G., Sonnenberg, A., Breakefield, X. O. (2008). TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton. J. Cell Sci. 121: 3476-3486 [Abstract] [Full Text]  
• Giles, L. M., Chen, J., Li, L., Chin, L.-S. (2008). Dystonia-associated mutations cause premature degradation of torsinA protein and cell-type-specific mislocalization to the nuclear envelope. Hum Mol Genet 17: 2712-2722 [Abstract] [Full Text]  
• Zhu, L., Wrabl, J. O., Hayashi, A. P., Rose, L. S., Thomas, P. J. (2008). The Torsin-family AAA+ Protein OOC-5 Contains a Critical Disulfide Adjacent to Sensor-II That Couples Redox State to Nucleotide Binding. Mol. Biol. Cell 19: 3599-3612 [Abstract] [Full Text]  
• Granata, A., Watson, R., Collinson, L. M., Schiavo, G., Warner, T. T. (2008). The Dystonia-associated Protein TorsinA Modulates Synaptic Vesicle Recycling. J. Biol. Chem. 283: 7568-7579 [Abstract] [Full Text]  
• Bengtsson, L., Otto, H. (2008). LUMA interacts with emerin and influences its distribution at the inner nuclear membrane. J. Cell Sci. 121: 536-548 [Abstract] [Full Text]  
• Hewett, J. W., Tannous, B., Niland, B. P., Nery, F. C., Zeng, J., Li, Y., Breakefield, X. O. (2007). Mutant torsinA interferes with protein processing through the secretory pathway in DYT1 dystonia cells. Proc. Natl. Acad. Sci. USA 104: 7271-7276 [Abstract] [Full Text]  
• Esapa, C. T., Waite, A., Locke, M., Benson, M. A., Kraus, M., McIlhinney, R.A. J., Sillitoe, R. V., Beesley, P. W., Blake, D. J. (2007). SGCE missense mutations that cause myoclonus-dystonia syndrome impair {varepsilon}-sarcoglycan trafficking to the plasma membrane: modulation by ubiquitination and torsinA. Hum Mol Genet 16: 327-342 [Abstract] [Full Text]  
• Kock, N., Naismith, T. V., Boston, H. E., Ozelius, L. J., Corey, D. P., Breakefield, X. O., Hanson, P. I. (2006). Effects of genetic variations in the dystonia protein torsinA: identification of polymorphism at residue 216 as protein modifier. Hum Mol Genet 15: 1355-1364 [Abstract] [Full Text]  
• Gindhart, J. G. (2006). Towards an understanding of kinesin-1 dependent transport pathways through the study of protein-protein interactions. Brief Funct Genomic Proteomic 5: 74-86 [Abstract] [Full Text]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents