Prenylation of oncogenic human PTPCAAX protein tyrosine phosphatases

Many isoprenylated proteins are known to participate in signal transduction, but not all have been identified. Using an in vitro prenylation screen, two human cDNAs (PTPCAAXI and PTPCAAX2) homologous to the rat PRL-1 and human OV-1 protein tyrosine phosphatase genes were identified. PTPCAAXI and PTP...

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Veröffentlicht in:Cancer letters 1996-12, Vol.110 (1-2), p.49-55
Hauptverfasser: CATES, C. A, MICHAEL, R. L, STAYROOK, K. R, HARVEY, K. A, BURKE, Y. D, RANDALL, S. K, CROWELL, P. L, CROWELL, D. N
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container_end_page 55
container_issue 1-2
container_start_page 49
container_title Cancer letters
container_volume 110
creator CATES, C. A
MICHAEL, R. L
STAYROOK, K. R
HARVEY, K. A
BURKE, Y. D
RANDALL, S. K
CROWELL, P. L
CROWELL, D. N
description Many isoprenylated proteins are known to participate in signal transduction, but not all have been identified. Using an in vitro prenylation screen, two human cDNAs (PTPCAAXI and PTPCAAX2) homologous to the rat PRL-1 and human OV-1 protein tyrosine phosphatase genes were identified. PTPCAAXI and PTPCAAX2 were farnesylated in vitro by mammalian farnesyl:protein transferase, and epitope-tagged PTPCAAX2 was prenylated in epithelial cells. Overexpression of PTPCAAXI and PTPCAAX2 in epithelial cells caused a transformed phenotype in culture and tumor growth in nude mice. Thus, PTPCAAXI and PTPCAAX2 represent a novel class of isoprenylated, oncogenic protein tyrosine phosphatases.
doi_str_mv 10.1016/s0304-3835(96)04459-x
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subjects Biological and medical sciences
Cell physiology
Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes
Fundamental and applied biological sciences. Psychology
Molecular and cellular biology
title Prenylation of oncogenic human PTPCAAX protein tyrosine phosphatases
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