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Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion.

Aricescu AR, Hon WC, Siebold C, Lu W, van der Merwe PA, Jones EY
EMBO J 25 701-12 (2006)
Cited: 65 times
EuropePMC logo PMID: 16456543

Abstract

Type IIB receptor protein tyrosine phosphatases (RPTPs) are bi-functional cell surface molecules. Their ectodomains mediate stable, homophilic, cell-adhesive interactions, whereas the intracellular catalytic regions can modulate the phosphorylation state of cadherin/catenin complexes. We describe a systematic investigation of the cell-adhesive properties of the extracellular region of RPTPmu, a prototypical type IIB RPTP. The crystal structure of a construct comprising its N-terminal MAM (meprin/A5/mu) and Ig domains was determined at 2.7 A resolution; this assigns the MAM fold to the jelly-roll family and reveals extensive interactions between the two domains, which form a rigid structural unit. Structure-based site-directed mutagenesis, serial domain deletions and cell-adhesion assays allowed us to identify the four N-terminal domains (MAM, Ig, fibronectin type III (FNIII)-1 and FNIII-2) as a minimal functional unit. Biophysical characterization revealed at least two independent types of homophilic interaction which, taken together, suggest that there is the potential for formation of a complex and possibly ordered array of receptor molecules at cell contact sites.

Articles - 2c9a mentioned but not cited (8)

  1. Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion. Aricescu AR, Hon WC, Siebold C, Lu W, van der Merwe PA, Jones EY. EMBO J 25 701-712 (2006)
  2. Structural Mechanism for Modulation of Synaptic Neuroligin-Neurexin Signaling by MDGA Proteins. Elegheert J, Cvetkovska V, Clayton AJ, Heroven C, Vennekens KM, Smukowski SN, Regan MC, Jia W, Smith AC, Furukawa H, Savas JN, de Wit J, Begbie J, Craig AM, Aricescu AR. Neuron 95 896-913.e10 (2017)
  3. Crystal Structure of the Neuropilin-1 MAM Domain: Completing the Neuropilin-1 Ectodomain Picture. Yelland T, Djordjevic S. Structure 24 2008-2015 (2016)
  4. Crystal structure of a Vip3B family insecticidal protein reveals a new fold and a unique tetrameric assembly. Zheng M, Evdokimov AG, Moshiri F, Lowder C, Haas J. Protein Sci 29 824-829 (2020)
  5. Targeting Neuroblastoma Cell Surface Proteins: Recommendations for Homology Modeling of hNET, ALK, and TrkB. Haddad Y, Heger Z, Adam V. Front Mol Neurosci 10 7 (2017)
  6. Suppressor Mutations in Type II Secretion Mutants of Vibrio cholerae: Inactivation of the VesC Protease. Rule CS, Park YJ, Delarosa JR, Turley S, Hol WGJ, McColm S, Gura C, DiMaio F, Korotkov KV, Sandkvist M. mSphere 5 e01125-20 (2020)
  7. The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins. Chakraborty S, Rendón-Ramírez A, Ásgeirsson B, Dutta M, Ghosh AS, Oda M, Venkatramani R, Rao BJ, Dandekar AM, Goñi FM. F1000Res 2 286 (2013)
  8. Binding Analysis of Sf-SR-C MAM Domain and Sf-FGFR Ectodomain to Vip3Aa. Wang C, Li M, Chen X, Fan S, Lan J. Insects 15 428 (2024)


Reviews citing this publication (17)

  1. Protein-tyrosine phosphatases and cancer. Ostman A, Hellberg C, Böhmer FD. Nat Rev Cancer 6 307-320 (2006)
  2. Meprins, membrane-bound and secreted astacin metalloproteinases. Sterchi EE, Stöcker W, Bond JS. Mol Aspects Med 29 309-328 (2008)
  3. Immunoglobulin superfamily cell adhesion molecules: zippers and signals. Aricescu AR, Jones EY. Curr Opin Cell Biol 19 543-550 (2007)
  4. Protein tyrosine phosphatases: structure-function relationships. Tabernero L, Aricescu AR, Jones EY, Szedlacsek SE. FEBS J 275 867-882 (2008)
  5. Targeting VEGF signalling via the neuropilin co-receptor. Djordjevic S, Driscoll PC. Drug Discov Today 18 447-455 (2013)
  6. Meprin A metalloproteinase and its role in acute kidney injury. Kaushal GP, Haun RS, Herzog C, Shah SV. Am J Physiol Renal Physiol 304 F1150-8 (2013)
  7. Expression of recombinant glycoproteins in mammalian cells: towards an integrative approach to structural biology. Aricescu AR, Owens RJ. Curr Opin Struct Biol 23 345-356 (2013)
  8. Tumour suppressor function of protein tyrosine phosphatase receptor-T. Scott A, Wang Z. Biosci Rep 31 303-307 (2011)
  9. Receptor-type tyrosine phosphatase ligands: looking for the needle in the haystack. Mohebiany AN, Nikolaienko RM, Bouyain S, Harroch S. FEBS J 280 388-400 (2013)
  10. Redox modifier genes and pathways in amyotrophic lateral sclerosis. Carter BJ, Anklesaria P, Choi S, Engelhardt JF. Antioxid Redox Signal 11 1569-1586 (2009)
  11. Regulation of development and cancer by the R2B subfamily of RPTPs and the implications of proteolysis. Craig SE, Brady-Kalnay SM. Semin Cell Dev Biol 37 108-118 (2015)
  12. Receptor protein tyrosine phosphatases and cancer: new insights from structural biology. Nikolaienko RM, Agyekum B, Bouyain S. Cell Adh Migr 6 356-364 (2012)
  13. Role of Neuropilin-1 in Diabetic Nephropathy. Bondeva T, Wolf G. J Clin Med 4 1293-1311 (2015)
  14. Phosphatase regulation of intercellular junctions. McCole DF. Tissue Barriers 1 e26713 (2013)
  15. Tumor-derived extracellular fragments of receptor protein tyrosine phosphatases (RPTPs) as cancer molecular diagnostic tools. Craig SE, Brady-Kalnay SM. Anticancer Agents Med Chem 11 133-140 (2011)
  16. High-throughput mutational analysis of the human cancer genome. Ma PC, Zhang X, Wang ZJ. Pharmacogenomics 7 597-612 (2006)
  17. Protein Tyrosine Phosphatases: A new paradigm in an old signaling system? Welsh CL, Pandey P, Ahuja LG. Adv Cancer Res 152 263-303 (2021)

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