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Molecular and Cellular Biology, April 2004, p. 3140-3149, Vol. 24, No. 8
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.8.3140-3149.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Generation and Characterization of LANP/pp32 Null Mice

Puneet Opal,1* Jesus J. Garcia,2 Alanna E. McCall,3 Bisong Xu,3 Edwin J. Weeber,4 J. David Sweatt,4 Harry T. Orr,5 and Huda Y. Zoghbi1,2,3,4

Departments of Neurology,1 Molecular and Human Genetics,3 Neuroscience,4 Howard Hughes Medical Institute, Baylor College of Medicine, Houston, Texas,2 Departments of Laboratory Medicine and Pathology and Biochemistry and Institute of Human Genetics, University of Minnesota, Minneapolis, Minnesota5

Received 25 September 2003/ Returned for modification 22 December 2003/ Accepted 23 January 2004

The leucine-rich acidic nuclear protein (LANP) belongs to a family of evolutionarily conserved proteins that are characterized by an amino-terminal domain rich in leucine residues followed by a carboxy-terminal acidic tail. LANP has been implicated in the regulation of a variety of cellular processes including RNA transport, transcription, apoptosis, vesicular trafficking, and intracellular signaling. Abundantly expressed in the developing cerebellum, this protein has also been hypothesized to play a role in cerebellar morphogenesis. LANP has been implicated in disease biology as well, both as a mediator of toxicity in spinocerebellar ataxia type 1 and as a tumor suppressor in cancers of the breast and prostate. To better understand the function of this multifaceted protein, we have generated mice lacking LANP. Surprisingly, these mice are viable and fertile. In addition we could not discern any derangements in any of the major organ systems, including the nervous system, which we have studied in detail. Overall our results point to a functional redundancy of LANP's function, most likely provided by its closely related family members.

* Corresponding author. Mailing address: Davee Dept. of Neurology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611. Phone: (312) 503-4699. Fax: (312) 503-0872. E-mail: p-opal{at}northwestern.edu.

Molecular and Cellular Biology, April 2004, p. 3140-3149, Vol. 24, No. 8
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.8.3140-3149.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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