Non-receptor-type putative protein tyrosine phosphatase-36 (PTP36), also known as PTPD2/Pez, possesses a domain homologous to the N-terminal half of band 4.1 protein. To gain insight into the biological function of PTP36, we established a HeLa cell line, HtTA/P36-9, in which the overexpression of PTP36 was inducible. PTP36 expressed in HeLa cells was enriched in the cytoskeleton near the plasma membrane. There was little endogenous PTP36 detectable in uninduced HtTA/P36-9 cells or in the parental HeLa cells. Upon induction of PTP36 overexpression, HtTA/P36-9 cells spread less well, grew more slowly, and adhered to the extracellular matrix proteins less well than uninduced cells. Moreover, decreases in the actin stress fibers and the number of focal adhesions were observed. The tyrosine phosphorylation of the focal adhesion kinase induced by lysophosphatidic acid was suppressed in the HtTA/P36-9 cells overexpressing PTP36. These results indicate that PTP36 affects cytoskeletons, cell adhesion, and cell growth, thus suggesting that PTP36 is involved in their regulatory processes.
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