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J Biol Chem, Vol. 274, Issue 26, 18559-18566, June 25, 1999

Phosphorylation at the Cyclin-dependent Kinases Site (Thr85) of Parathyroid Hormone-related Protein Negatively Regulates Its Nuclear Localization

Mark H. C. Lam, Colin M. House, Tony Tiganis, Ken I. Mitchelhill, Boris Sarcevic, Alina Curesparallel , Robert Ramsayparallel , Bruce E. Kemp, T. John Martin, and Matthew T. Gillespie

From the St. Vincent's Institute of Medical Research and the Department of Medicine, The University of Melbourne, 41 Victoria Parade, Fitzroy, Victoria 3065, Australia, the  Cancer Research Program, The Garvan Institute of Medical Research, St. Vincent's Hospital, 384 Victoria Street, Darlinghurst, Sydney, New South Wales 2010, Australia, and parallel  The Peter MacCallum Cancer Institute, St. Andrew's Place, East Melbourne, Victoria 3002, Australia

Parathyroid hormone-related protein (PTHrP) is expressed by a wide variety of cells and is considered to act as a secreted factor; however, evidence is accumulating for it to act in an intracrine manner. We have determined that PTHrP localizes to the nucleus at the G1 phase of the cell cycle and is transported to the cytoplasm when cells divide. PTHrP contains a putative nuclear localization sequence (NLS) (residues 61-94) similar to that of SV40 T-antigen, which may be implicated in the nuclear import of the molecule. We identified that Thr85 immediately prior to the NLS of PTHrP was phosphorylated by CDC2-CDK2 and phosphorylation was cell cycle-dependent. Mutation of Thr85 to Ala85 resulted in nuclear accumulation of PTHrP, while mutation to Glu85 to mimic a phosphorylated residue resulted in localization of PTHrP to the cytoplasm. Combined, the data demonstrate that the intracellular localization of PTHrP is phosphorylation- and cell cycle-dependent, and such control further supports a potential intracellular role (10, 34, 35) for PTHrP.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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