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M112112200v1
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Papers In Press, published online ahead of print March 6, 2002
J. Biol. Chem, 10.1074/jbc.M112112200
Submitted on December 19, 2001
Revised on February 22, 2002
Accepted on March 6, 2002

Identification of a karyopherin alpha 2 recognition site in PLAG1, which functions as a nuclear localization signal

Caroline V. Braem, Koen Kas, Eva Meyen, Maria Debiec-Rychter, Wim J.M. Van de Ven, and Marianne L. Voz

Department of Human Genetics, University of Leuven, Leuven, Vlaams-Brabant B-3000

Corresponding Author: caroline.braem{at}med.kuleuven.ac.be

Activation of the PLAG1 gene is the most frequent gain-of-function mutation found in pleomorphic adenomas of the salivary glands. To gain more insights into the regulation of PLAG1 function, we searched for PLAG1 interacting proteins. Using the yeast-two-hybrid system, we identified karyopherin alpha 2 (Kpna2), as a PLAG1-interacting protein. Physical interaction between PLAG1 and karyopherin alpha 2 was confirmed by an in vitro glutathione S-transferase (GST) pulldown assay. Karyopherin alpha 2 escorts proteins into the nucleus via interaction with a nuclear localization sequence (NLS) composed of short stretches of basic amino acids. Two putative NLSs were identified in PLAG1. The predicted NLS1 (KRKR) was essential for physical interaction with karyopherin alpha 2 in GST pulldown and its mutation resulted in decreased nuclear import of PLAG1. Moreover, NLS1 was able to drive the nuclear import of the cytoplasmic protein beta -galactosidase. In contrast, predicted NLS2 of PLAG1 (KPRK) was not involved in karyopherin alpha 2 binding, nor in its nuclear import. The residual nuclear import of PLAG1 after mutation of the NLS1 was assigned to the zinc finger domain of PLAG1. These observations indicate that the nuclear import of PLAG1 is governed by its zinc finger domain and by NLS1, a karyopherin alpha 2 recognition site.


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