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Protein tyrosine phosphatase type IVA 3 is an enzyme that in humans is encoded by the PTP4A3gene.[5]
The protein encoded by this gene belongs to a small class of prenylated protein tyrosine phosphatases (PTPs). PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. This class of PTPs contain a PTP domain and a characteristic C-terminal prenylation motif. Studies of this class of PTPs in mice demonstrated that they were prenylated proteins in vivo, which suggested their association with cell plasma membrane. Overexpression of this gene in mammalian cells was reported to inhibit angiotensin-II induced cell calcium mobilization and promote cell growth. Two alternatively spliced variants exist.[5]
Zeng Q, Hong W, Tan YH (1998). "Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1". Biochem. Biophys. Res. Commun. 244 (2): 421–7. doi:10.1006/bbrc.1998.8291. PMID9514946.
Dayton MA, Knobloch TJ (1998). "Multiple phosphotyrosine phosphatase mRNAs are expressed in the human lung fibroblast cell line WI-38". Receptors & Signal Transduction. 7 (4): 241–56. PMID9633825.
Pathak MK, Dhawan D, Lindner DJ, et al. (2003). "Pentamidine is an inhibitor of PRL phosphatases with anticancer activity". Mol. Cancer Ther. 1 (14): 1255–64. PMID12516958.
Zeng Q, Dong JM, Guo K, et al. (2003). "PRL-3 and PRL-1 promote cell migration, invasion, and metastasis". Cancer Res. 63 (11): 2716–22. PMID12782572.
Bardelli A, Saha S, Sager JA, et al. (2004). "PRL-3 expression in metastatic cancers". Clin. Cancer Res. 9 (15): 5607–15. PMID14654542.
Peng L, Jin G, Wang L, et al. (2006). "Identification of integrin alpha1 as an interacting protein of protein tyrosine phosphatase PRL-3". Biochem. Biophys. Res. Commun. 342 (1): 179–83. doi:10.1016/j.bbrc.2006.01.102. PMID16472776.