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Gene Review

Acp1  -  acid phosphatase 1, soluble

Mus musculus

Synonyms: 4632432E04Rik, AI427468, Acp-1, LMW-PTP, LMW-PTPase, ...
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Disease relevance of Acp1


High impact information on Acp1


Biological context of Acp1

  • On the basis of these results, we propose a key role for LMW-PTP in PDGF-r down-regulation through the dephosphorylation of the activation loop Tyr-857, thus determining a general negative regulation of all downstream signals, with the exception of those elicited by internalized receptors [10].
  • The low molecular weight protein-tyrosine phosphatase (LMW-PTP) is an enzyme that is involved in the early events of platelet-derived growth factor (PDGF) receptor signal transduction [11].
  • It contains both an intrinsic protein tyrosine phosphatase (PTPase) activity and a cytoskeleton binding site in its cytoplasmic domain [12].
  • In particular, LMW-PTP is involved in pathways that regulate the transcription of the immediately early genes myc and fos in response to growth factor stimulation [11].
  • Constitutive expression of the PTPase by 3T3-L1 preadipocytes using a PTPase HA2 expression vector prevents adipocyte gene expression and differentiation into adipocytes [13].

Anatomical context of Acp1


Associations of Acp1 with chemical compounds


Regulatory relationships of Acp1


Other interactions of Acp1


Analytical, diagnostic and therapeutic context of Acp1


  1. The Yersinia tyrosine phosphatase: specificity of a bacterial virulence determinant for phosphoproteins in the J774A.1 macrophage. Bliska, J.B., Clemens, J.C., Dixon, J.E., Falkow, S. J. Exp. Med. (1992) [Pubmed]
  2. Receptor protein tyrosine phosphatase alpha activates pp60c-src and is involved in neuronal differentiation. den Hertog, J., Pals, C.E., Peppelenbosch, M.P., Tertoolen, L.G., de Laat, S.W., Kruijer, W. EMBO J. (1993) [Pubmed]
  3. Inactivation of raf-1 by a protein-tyrosine phosphatase stimulated by GTP and reconstituted by Galphai/o subunits. Dent, P., Reardon, D.B., Wood, S.L., Lindorfer, M.A., Graber, S.G., Garrison, J.C., Brautigan, D.L., Sturgill, T.W. J. Biol. Chem. (1996) [Pubmed]
  4. Protein tyrosine phosphatase-dependent activation of beta-globin and delta-aminolevulinic acid synthase genes in the camptothecin-induced IW32 erythroleukemia cell differentiation. Wang, M.C., Liu, J.H., Wang, F.F. Mol. Pharmacol. (1997) [Pubmed]
  5. Induction of specific protein tyrosine phosphatase transcripts during differentiation of mouse embryonal carcinoma (F9) cells. Tsuneizumi, K., Kume, T., Watanabe, T., Gebbink, M.F., Thomas, M.L., Oishi, M. FEBS Lett. (1994) [Pubmed]
  6. CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling. Irie-Sasaki, J., Sasaki, T., Matsumoto, W., Opavsky, A., Cheng, M., Welstead, G., Griffiths, E., Krawczyk, C., Richardson, C.D., Aitken, K., Iscove, N., Koretzky, G., Johnson, P., Liu, P., Rothstein, D.M., Penninger, J.M. Nature (2001) [Pubmed]
  7. Negative regulation of CD45 protein tyrosine phosphatase activity by ionomycin in T cells. Ostergaard, H.L., Trowbridge, I.S. Science (1991) [Pubmed]
  8. Vanadate normalizes hyperglycemia in two mouse models of non-insulin-dependent diabetes mellitus. Meyerovitch, J., Rothenberg, P., Shechter, Y., Bonner-Weir, S., Kahn, C.R. J. Clin. Invest. (1991) [Pubmed]
  9. Tyrosine phosphate hydrolysis of host proteins by an essential Yersinia virulence determinant. Bliska, J.B., Guan, K.L., Dixon, J.E., Falkow, S. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  10. Insight into the role of low molecular weight phosphotyrosine phosphatase (LMW-PTP) on platelet-derived growth factor receptor (PDGF-r) signaling. LMW-PTP controls PDGF-r kinase activity through TYR-857 dephosphorylation. Chiarugi, P., Cirri, P., Taddei, M.L., Giannoni, E., Fiaschi, T., Buricchi, F., Camici, G., Raugei, G., Ramponi, G. J. Biol. Chem. (2002) [Pubmed]
  11. The low M(r) protein-tyrosine phosphatase is involved in Rho-mediated cytoskeleton rearrangement after integrin and platelet-derived growth factor stimulation. Chiarugi, P., Cirri, P., Taddei, L., Giannoni, E., Camici, G., Manao, G., Raugei, G., Ramponi, G. J. Biol. Chem. (2000) [Pubmed]
  12. Mapping the fodrin binding domain in CD45, a leukocyte membrane-associated tyrosine phosphatase. Iida, N., Lokeshwar, V.B., Bourguignon, L.Y. J. Biol. Chem. (1994) [Pubmed]
  13. The blockade of preadipocyte differentiation by protein-tyrosine phosphatase HA2 is reversed by vanadate. Liao, K., Lane, M.D. J. Biol. Chem. (1995) [Pubmed]
  14. The Src and signal transducers and activators of transcription pathways as specific targets for low molecular weight phosphotyrosine-protein phosphatase in platelet-derived growth factor signaling. Chiarugi, P., Cirri, P., Marra, F., Raugei, G., Fiaschi, T., Camici, G., Manao, G., Romanelli, R.G., Ramponi, G. J. Biol. Chem. (1998) [Pubmed]
  15. c-Crk, a substrate of the insulin-like growth factor-1 receptor tyrosine kinase, functions as an early signal mediator in the adipocyte differentiation process. Jin, S., Zhai, B., Qiu, Z., Wu, J., Lane, M.D., Liao, K. J. Biol. Chem. (2000) [Pubmed]
  16. Expression of a transmembrane phosphotyrosine phosphatase inhibits cellular response to platelet-derived growth factor and insulin-like growth factor-1. Mooney, R.A., Freund, G.G., Way, B.A., Bordwell, K.L. J. Biol. Chem. (1992) [Pubmed]
  17. Tyrosine kinase and CD45 tyrosine phosphatase activity mediate p21ras activation in B cells stimulated through the antigen receptor. Kawauchi, K., Lazarus, A.H., Rapoport, M.J., Harwood, A., Cambier, J.C., Delovitch, T.L. J. Immunol. (1994) [Pubmed]
  18. Mutational analysis of CD45. A leukocyte-specific protein tyrosine phosphatase. Johnson, P., Ostergaard, H.L., Wasden, C., Trowbridge, I.S. J. Biol. Chem. (1992) [Pubmed]
  19. Sodium stibogluconate is a potent inhibitor of protein tyrosine phosphatases and augments cytokine responses in hemopoietic cell lines. Pathak, M.K., Yi, T. J. Immunol. (2001) [Pubmed]
  20. The protein tyrosine phosphatase Shp-2 regulates RhoA activity. Schoenwaelder, S.M., Petch, L.A., Williamson, D., Shen, R., Feng, G.S., Burridge, K. Curr. Biol. (2000) [Pubmed]
  21. S49 cells endogenously express subtype 2 somatostatin receptors which couple to increase protein tyrosine phosphatase activity in membranes and down-regulate Raf-1 activity in situ. Dent, P., Wang, Y., Gu, Y.Z., Wood, S.L., Reardon, D.B., Mangues, R., Pellicer, A., Schonbrunn, A., Sturgill, T.W. Cell. Signal. (1997) [Pubmed]
  22. Effects of hemizygous CD45 expression in the autoimmune Fasl(gld/gld) syndrome. Brooks, W.P., Lynes, M.A. Cell. Immunol. (2001) [Pubmed]
  23. Transgenic mice deficient in the LAR protein-tyrosine phosphatase exhibit profound defects in glucose homeostasis. Ren, J.M., Li, P.M., Zhang, W.R., Sweet, L.J., Cline, G., Shulman, G.I., Livingston, J.N., Goldstein, B.J. Diabetes (1998) [Pubmed]
  24. The phosphotyrosine phosphatase inhibitor-phenylarsine oxide restores defective phosphoinositide hydrolysis response in anergic C3H-gld/gld lymphocytes. Ling, W., Tibbetts, D.J., Crain, R.C., Lynes, M.A. Immunol. Cell Biol. (1996) [Pubmed]
  25. Induction of protein tyrosine phosphatase epsilon transcripts during NGF-induced neuronal differentiation of PC12D cells and during the development of the cerebellum. Mukouyama, Y., Kuroyanagi, H., Shirasawa, T., Tomoda, T., Saffen, D., Oishi, M., Watanabe, T. Brain Res. Mol. Brain Res. (1997) [Pubmed]
  26. A novel receptor-type protein tyrosine phosphatase with a single catalytic domain is specifically expressed in mouse brain. Hendriks, W., Schepens, J., Brugman, C., Zeeuwen, P., Wieringa, B. Biochem. J. (1995) [Pubmed]
  27. Protein-tyrosine phosphatases expressed in mouse epidermal keratinocytes. Hendriks, W., Brugman, C., Richter, K.H., van Hooijdonk, C., Schepens, J., Schalkwijk, J., Wieringa, B. J. Invest. Dermatol. (1996) [Pubmed]
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