2dle: Difference between revisions

Revision as of 06:08, 30 May 2018

Solution structure of the fourth fn3 domain of human receptor-type tyrosine-protein phosphatase eta

Structural highlights

2dle is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	PTPRJ, DEP1 (HUMAN)
Activity:	Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[PTPRJ_HUMAN] Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, RET (variant MEN2A), KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2. Plays a role in cell adhesion, migration, proliferation and differentiation. Involved in vascular development. Regulator of macrophage adhesion and spreading. Positively affects cell-matrix adhesion. Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation. Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR. Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation. Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation. Enhances the barrier function of epithelial junctions during reassembly. Negatively regulates T-cell receptor (TCR) signaling. Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9] ^[10] ^[11] ^[12] ^[13] ^[14] ^[15] ^[16] ^[17] ^[18] ^[19]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ de la Fuente-Garcia MA, Nicolas JM, Freed JH, Palou E, Thomas AP, Vilella R, Vives J, Gaya A. CD148 is a membrane protein tyrosine phosphatase present in all hematopoietic lineages and is involved in signal transduction on lymphocytes. Blood. 1998 Apr 15;91(8):2800-9. PMID:9531590
↑ Tangye SG, Wu J, Aversa G, de Vries JE, Lanier LL, Phillips JH. Negative regulation of human T cell activation by the receptor-type protein tyrosine phosphatase CD148. J Immunol. 1998 Oct 15;161(8):3803-7. PMID:9780142
↑ Kovalenko M, Denner K, Sandstrom J, Persson C, Gross S, Jandt E, Vilella R, Bohmer F, Ostman A. Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1. J Biol Chem. 2000 May 26;275(21):16219-26. PMID:10821867
↑ Baker JE, Majeti R, Tangye SG, Weiss A. Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation. Mol Cell Biol. 2001 Apr;21(7):2393-403. PMID:11259588 doi:https://dx.doi.org/10.1128/MCB.21.7.2393-2403.2001
↑ Persson C, Engstrom U, Mowbray SL, Ostman A. Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1. FEBS Lett. 2002 Apr 24;517(1-3):27-31. PMID:12062403
↑ Holsinger LJ, Ward K, Duffield B, Zachwieja J, Jallal B. The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn). Oncogene. 2002 Oct 10;21(46):7067-76. PMID:12370829 doi:https://dx.doi.org/10.1038/sj.onc.1205858
↑ Palka HL, Park M, Tonks NK. Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1. J Biol Chem. 2003 Feb 21;278(8):5728-35. Epub 2002 Dec 9. PMID:12475979 doi:https://dx.doi.org/10.1074/jbc.M210656200
↑ Lin J, Weiss A. The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling. J Cell Biol. 2003 Aug 18;162(4):673-82. Epub 2003 Aug 11. PMID:12913111 doi:https://dx.doi.org/10.1083/jcb.200303040
↑ Kellie S, Craggs G, Bird IN, Jones GE. The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation. J Cell Sci. 2004 Feb 1;117(Pt 4):609-18. Epub 2004 Jan 6. PMID:14709717 doi:https://dx.doi.org/10.1242/jcs.00879
↑ Iervolino A, Iuliano R, Trapasso F, Viglietto G, Melillo RM, Carlomagno F, Santoro M, Fusco A. The receptor-type protein tyrosine phosphatase J antagonizes the biochemical and biological effects of RET-derived oncoproteins. Cancer Res. 2006 Jun 15;66(12):6280-7. PMID:16778204 doi:https://dx.doi.org/10.1158/0008-5472.CAN-06-0228
↑ Balavenkatraman KK, Jandt E, Friedrich K, Kautenburger T, Pool-Zobel BL, Ostman A, Bohmer FD. DEP-1 protein tyrosine phosphatase inhibits proliferation and migration of colon carcinoma cells and is upregulated by protective nutrients. Oncogene. 2006 Oct 12;25(47):6319-24. Epub 2006 May 8. PMID:16682945 doi:https://dx.doi.org/10.1038/sj.onc.1209647
↑ Tsuboi N, Utsunomiya T, Roberts RL, Ito H, Takahashi K, Noda M, Takahashi T. The tyrosine phosphatase CD148 interacts with the p85 regulatory subunit of phosphoinositide 3-kinase. Biochem J. 2008 Jul 1;413(1):193-200. doi: 10.1042/BJ20071317. PMID:18348712 doi:https://dx.doi.org/10.1042/BJ20071317
↑ Tarcic G, Boguslavsky SK, Wakim J, Kiuchi T, Liu A, Reinitz F, Nathanson D, Takahashi T, Mischel PS, Ng T, Yarden Y. An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis. Curr Biol. 2009 Nov 17;19(21):1788-98. doi: 10.1016/j.cub.2009.09.048. PMID:19836242 doi:https://dx.doi.org/10.1016/j.cub.2009.09.048
↑ Sallee JL, Burridge K. Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells. J Biol Chem. 2009 May 29;284(22):14997-5006. doi: 10.1074/jbc.M901901200. Epub, 2009 Mar 30. PMID:19332538 doi:https://dx.doi.org/10.1074/jbc.M901901200
↑ Sacco F, Tinti M, Palma A, Ferrari E, Nardozza AP, Hooft van Huijsduijnen R, Takahashi T, Castagnoli L, Cesareni G. Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS pathway by direct dephosphorylation of ERK1/2 kinases. J Biol Chem. 2009 Aug 14;284(33):22048-58. doi: 10.1074/jbc.M109.002758. Epub, 2009 Jun 3. PMID:19494114 doi:https://dx.doi.org/10.1074/jbc.M109.002758
↑ Chabot C, Spring K, Gratton JP, Elchebly M, Royal I. New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival. Mol Cell Biol. 2009 Jan;29(1):241-53. doi: 10.1128/MCB.01374-08. Epub 2008 Oct, 20. PMID:18936167 doi:https://dx.doi.org/10.1128/MCB.01374-08
↑ Petermann A, Haase D, Wetzel A, Balavenkatraman KK, Tenev T, Guhrs KH, Friedrich S, Nakamura M, Mawrin C, Bohmer FD. Loss of the protein-tyrosine phosphatase DEP-1/PTPRJ drives meningioma cell motility. Brain Pathol. 2011 Jul;21(4):405-18. doi: 10.1111/j.1750-3639.2010.00464.x. Epub , 2010 Dec 27. PMID:21091576 doi:https://dx.doi.org/10.1111/j.1750-3639.2010.00464.x
↑ Omerovic J, Clague MJ, Prior IA. Phosphatome profiling reveals PTPN2, PTPRJ and PTEN as potent negative regulators of PKB/Akt activation in Ras-mutated cancer cells. Biochem J. 2010 Jan 27;426(1):65-72. doi: 10.1042/BJ20091413. PMID:19922411 doi:https://dx.doi.org/10.1042/BJ20091413
↑ Arora D, Stopp S, Bohmer SA, Schons J, Godfrey R, Masson K, Razumovskaya E, Ronnstrand L, Tanzer S, Bauer R, Bohmer FD, Muller JP. Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3 signaling. J Biol Chem. 2011 Apr 1;286(13):10918-29. doi: 10.1074/jbc.M110.205021. Epub 2011, Jan 24. PMID:21262971 doi:10.1074/jbc.M110.205021

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Fuente-Garcia MA, Nicolas JM, Freed JH, Palou E, Thomas AP, Vilella R, Vives J, Gaya A. CD148 is a membrane protein tyrosine phosphatase present in all hematopoietic lineages and is involved in signal transduction on lymphocytes. Blood. 1998 Apr 15;91(8):2800-9. PMID:9531590

[2] Tangye SG, Wu J, Aversa G, de Vries JE, Lanier LL, Phillips JH. Negative regulation of human T cell activation by the receptor-type protein tyrosine phosphatase CD148. J Immunol. 1998 Oct 15;161(8):3803-7. PMID:9780142

[3] Kovalenko M, Denner K, Sandstrom J, Persson C, Gross S, Jandt E, Vilella R, Bohmer F, Ostman A. Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1. J Biol Chem. 2000 May 26;275(21):16219-26. PMID:10821867

[4] Baker JE, Majeti R, Tangye SG, Weiss A. Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation. Mol Cell Biol. 2001 Apr;21(7):2393-403. PMID:11259588 doi:https://dx.doi.org/10.1128/MCB.21.7.2393-2403.2001

[5] Persson C, Engstrom U, Mowbray SL, Ostman A. Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1. FEBS Lett. 2002 Apr 24;517(1-3):27-31. PMID:12062403

[6] Holsinger LJ, Ward K, Duffield B, Zachwieja J, Jallal B. The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn). Oncogene. 2002 Oct 10;21(46):7067-76. PMID:12370829 doi:https://dx.doi.org/10.1038/sj.onc.1205858

[7] Palka HL, Park M, Tonks NK. Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1. J Biol Chem. 2003 Feb 21;278(8):5728-35. Epub 2002 Dec 9. PMID:12475979 doi:https://dx.doi.org/10.1074/jbc.M210656200

[8] Lin J, Weiss A. The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling. J Cell Biol. 2003 Aug 18;162(4):673-82. Epub 2003 Aug 11. PMID:12913111 doi:https://dx.doi.org/10.1083/jcb.200303040

[9] Kellie S, Craggs G, Bird IN, Jones GE. The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation. J Cell Sci. 2004 Feb 1;117(Pt 4):609-18. Epub 2004 Jan 6. PMID:14709717 doi:https://dx.doi.org/10.1242/jcs.00879

[10] Iervolino A, Iuliano R, Trapasso F, Viglietto G, Melillo RM, Carlomagno F, Santoro M, Fusco A. The receptor-type protein tyrosine phosphatase J antagonizes the biochemical and biological effects of RET-derived oncoproteins. Cancer Res. 2006 Jun 15;66(12):6280-7. PMID:16778204 doi:https://dx.doi.org/10.1158/0008-5472.CAN-06-0228

[11] Balavenkatraman KK, Jandt E, Friedrich K, Kautenburger T, Pool-Zobel BL, Ostman A, Bohmer FD. DEP-1 protein tyrosine phosphatase inhibits proliferation and migration of colon carcinoma cells and is upregulated by protective nutrients. Oncogene. 2006 Oct 12;25(47):6319-24. Epub 2006 May 8. PMID:16682945 doi:https://dx.doi.org/10.1038/sj.onc.1209647

[12] Tsuboi N, Utsunomiya T, Roberts RL, Ito H, Takahashi K, Noda M, Takahashi T. The tyrosine phosphatase CD148 interacts with the p85 regulatory subunit of phosphoinositide 3-kinase. Biochem J. 2008 Jul 1;413(1):193-200. doi: 10.1042/BJ20071317. PMID:18348712 doi:https://dx.doi.org/10.1042/BJ20071317

[13] Tarcic G, Boguslavsky SK, Wakim J, Kiuchi T, Liu A, Reinitz F, Nathanson D, Takahashi T, Mischel PS, Ng T, Yarden Y. An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis. Curr Biol. 2009 Nov 17;19(21):1788-98. doi: 10.1016/j.cub.2009.09.048. PMID:19836242 doi:https://dx.doi.org/10.1016/j.cub.2009.09.048

[14] Sallee JL, Burridge K. Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells. J Biol Chem. 2009 May 29;284(22):14997-5006. doi: 10.1074/jbc.M901901200. Epub, 2009 Mar 30. PMID:19332538 doi:https://dx.doi.org/10.1074/jbc.M901901200

[15] Sacco F, Tinti M, Palma A, Ferrari E, Nardozza AP, Hooft van Huijsduijnen R, Takahashi T, Castagnoli L, Cesareni G. Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS pathway by direct dephosphorylation of ERK1/2 kinases. J Biol Chem. 2009 Aug 14;284(33):22048-58. doi: 10.1074/jbc.M109.002758. Epub, 2009 Jun 3. PMID:19494114 doi:https://dx.doi.org/10.1074/jbc.M109.002758

[16] Chabot C, Spring K, Gratton JP, Elchebly M, Royal I. New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival. Mol Cell Biol. 2009 Jan;29(1):241-53. doi: 10.1128/MCB.01374-08. Epub 2008 Oct, 20. PMID:18936167 doi:https://dx.doi.org/10.1128/MCB.01374-08

[17] Petermann A, Haase D, Wetzel A, Balavenkatraman KK, Tenev T, Guhrs KH, Friedrich S, Nakamura M, Mawrin C, Bohmer FD. Loss of the protein-tyrosine phosphatase DEP-1/PTPRJ drives meningioma cell motility. Brain Pathol. 2011 Jul;21(4):405-18. doi: 10.1111/j.1750-3639.2010.00464.x. Epub , 2010 Dec 27. PMID:21091576 doi:https://dx.doi.org/10.1111/j.1750-3639.2010.00464.x

[18] Omerovic J, Clague MJ, Prior IA. Phosphatome profiling reveals PTPN2, PTPRJ and PTEN as potent negative regulators of PKB/Akt activation in Ras-mutated cancer cells. Biochem J. 2010 Jan 27;426(1):65-72. doi: 10.1042/BJ20091413. PMID:19922411 doi:https://dx.doi.org/10.1042/BJ20091413

[19] Arora D, Stopp S, Bohmer SA, Schons J, Godfrey R, Masson K, Razumovskaya E, Ronnstrand L, Tanzer S, Bauer R, Bohmer FD, Muller JP. Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3 signaling. J Biol Chem. 2011 Apr 1;286(13):10918-29. doi: 10.1074/jbc.M110.205021. Epub 2011, Jan 24. PMID:21262971 doi:10.1074/jbc.M110.205021

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@@ Line 1: / Line 1: @@
 ==Solution structure of the fourth fn3 domain of human receptor-type tyrosine-protein phosphatase eta==
 <StructureSection load='2dle' size='340' side='right' caption='[[2dle]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPRJ, DEP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dle OCA], [http://pdbe.org/2dle PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dle RCSB], [http://www.ebi.ac.uk/pdbsum/2dle PDBsum], [http://www.topsan.org/Proteins/RSGI/2dle TOPSAN]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dle OCA], [http://pdbe.org/2dle PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dle RCSB], [http://www.ebi.ac.uk/pdbsum/2dle PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dle ProSAT], [http://www.topsan.org/Proteins/RSGI/2dle TOPSAN]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dl/2dle_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dl/2dle_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2dle ConSurf].
 <div style="clear:both"></div>

2dle: Difference between revisions

Revision as of 06:08, 30 May 2018

Solution structure of the fourth fn3 domain of human receptor-type tyrosine-protein phosphatase eta

Structural highlights

Function

Evolutionary Conservation

See Also

References

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