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Molecular and Cellular Biology, June 2004, p. 5324-5331, Vol. 24, No. 12
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.12.5324-5331.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The TALE Homeodomain Protein Pbx2 Is Not Essential for Development and Long-Term Survival

Licia Selleri,1* Jorge DiMartino,1 Jan van Deursen,3 Andrea Brendolan,2 Mrinmoy Sanyal,1 Elles Boon,1 Terence Capellini,2 Kevin S. Smith,1 Joon Rhee,1 Heike Pöpperl,4 Gerard Grosveld,5 and Michael L. Cleary1*

Department of Pathology, Stanford University School of Medicine, Stanford, California 94305,1 Institute of Genetic Medicine, Cornell University Weill Medical School, New York, New York 10021,2 Pediatrics and Adolescent Medicine, Mayo Clinic, Rochester, Minnesota 55905,3 Deutsches Krebsforchungszentrum, Angewandte Tumorvirologie, 69120 Heidelberg, Germany,4 Department of Genetics, St. Jude Children's Research Hospital, Memphis, Tennessee 381055

Received 31 October 2003/ Returned for modification 8 December 2003/ Accepted 18 March 2004

Pbx2 is one of four mammalian genes that encode closely related TALE homeodomain proteins, which serve as DNA binding partners for a subset of Hox transcription factors. The expression and contributions of Pbx2 to mammalian development remain undefined, in contrast to the essential roles recently established for family members Pbx1 and Pbx3. Here we report that Pbx2 is widely expressed during embryonic development, particularly in neural and epithelial tissues during late gestation. Despite wide Pbx2 expression, mice homozygous mutant for Pbx2 are born at the expected Mendelian frequencies and exhibit no detectable abnormalities in development and organogenesis or reduction of long-term survival. The lack of an apparent phenotype in Pbx2–/– mice likely reflects functional redundancy, since the Pbx2 protein is present at considerably lower levels than comparable isoforms of Pbx1 and/or Pbx3 in embryonic tissues. In postnatal bone marrow and thymus, however, Pbx2 is the predominant high-molecular-weight (MW)-isoform Pbx protein detectable by immunoblotting. Nevertheless, the absence of Pbx2 has no measurable effect on steady-state hematopoiesis or immune function in adult mice, suggesting possible compensation by low-MW-isoform Pbx proteins present in these tissues. We conclude that the roles of Pbx2 in murine embryonic development, organogenesis, hematopoiesis, immune responses, and long-term survival are not essential.

* Corresponding author. Mailing address for Michael L. Cleary: Department of Pathology, Stanford University School of Medicine, 300 Pasteur Dr., Stanford, CA 94305-5342. Phone: (650) 723-5471. Fax: (650) 498-6222. E-mail: mcleary{at}stanford.edu. Mailing address for Licia Selleri: Molecular Biology Program, Cornell University/Sloan-Kettering Institute, Institute of Genetic Medicine, Whitney Tower, W-406, Cornell University Medical School, 1300 York Ave., New York, NY 10021. Phone: (212) 746-5009. Fax: (212) 746-8824. E-mail: lis2008{at}med.cornell.edu.

Molecular and Cellular Biology, June 2004, p. 5324-5331, Vol. 24, No. 12
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.12.5324-5331.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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