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J Biol Chem, Vol. 273, Issue 33, 21077-21083, August 14, 1998

A Novel Putative Protein-tyrosine Phosphatase Contains a BRO1-like Domain and Suppresses Ha-ras-mediated Transformation

Linguang Cao, Li Zhang, Pilar Ruiz-Lozano^§, Qicheng Yang^¶, Kenneth R. Chien^§, Robert M. Graham, and Mingdong Zhou

 Victor Chang Cardiac Research Institute, St. Vincent's Hospital, Darlinghurst, NSW 2010, Australia,  School of Biochemistry and Molecular Genetics, The University of New South Wales, Kensington, NSW 2052 Australia, ^§ School of Medicine, University of California, San Diego, La Jolla, California 92093, and ^¶ Immusol Inc., San Diego, California 92121

To investigate a potential role of protein-tyrosine phosphatases (PTPases) in myocardial growth and signaling, a degenerate primer-based reverse transcription-polymerase chain reaction approach was used to isolate cDNAs for proteins that contain a PTPase catalytic domain. Among the 16 cDNA clones isolated by reverse transcription-polymerase chain reaction from total neonatal rat cardiomyocyte RNA, one, designated PTP-TD14, was unique. Subsequent isolation and sequencing of a full-length PTP-TD14 cDNA confirmed that it encodes a novel 164-kDa protein, p164^PTP-TD14. The C-terminal region contains the PTP-like domain, whereas the N-terminal region shows no homology to any known mammalian protein. However, this region is homologous to a yeast protein, BRO1, that is involved in the mitogen-activated protein kinase signaling pathway. Like BRO1, p164^PTP-TD14 contains a proline-rich region with two putative SH3-domain binding sites. By Northern blot analysis, PTP-TD14 is expressed as a 5.3-kilobase pair transcript, not only in neonatal heart but also in many adult rat tissues. When expressed in either COS-7 or NIH-3T3 cells, p164^PTP-TD14 localizes to the cytoplasm in association with vesicle-like structures. Expression of p164^PTP-TD14 in NIH-3T3 cells inhibits Ha-ras-mediated transformation more than 3-fold. This inhibitory activity is localized to the C-terminal PTPase homology domain, since no inhibition of Ha-ras-mediated focus formation was observed with a PTP-TD14 mutant, in which the putative catalytic activity was presumably inactivated by a point mutation. These findings indicate that PTP-TD14 encodes a novel protein that may be critically involved in regulating Ha-ras-dependent cell growth.

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