User menu

A unique C-terminal domain allows retention of matrix metalloproteinase-27 in the endoplasmic reticulum

Bibliographic reference Cominelli, Antoine ; Halbout, Mathias ; N'Kuli, Francisca ; Lemoine, Pascale ; Courtoy, Pierre J. ; et. al. A unique C-terminal domain allows retention of matrix metalloproteinase-27 in the endoplasmic reticulum. In: Traffic, Vol. 15, no. 4, p. 401-417 (2014)
Permanent URL
  1. Page-McCaw Andrea, Ewald Andrew J., Werb Zena, Matrix metalloproteinases and the regulation of tissue remodelling, 10.1038/nrm2125
  2. Rodríguez David, Morrison Charlotte J., Overall Christopher M., Matrix metalloproteinases: What do they not do? New substrates and biological roles identified by murine models and proteomics, 10.1016/j.bbamcr.2009.09.015
  3. NAGASE H, VISSE R, MURPHY G, Structure and function of matrix metalloproteinases and TIMPs, 10.1016/j.cardiores.2005.12.002
  4. Gaide Chevronnay Héloïse P., Selvais Charlotte, Emonard Hervé, Galant Christine, Marbaix Etienne, Henriet Patrick, Regulation of matrix metalloproteinases activity studied in human endometrium as a paradigm of cyclic tissue breakdown and regeneration, 10.1016/j.bbapap.2011.09.003
  5. Kessenbrock Kai, Plaks Vicki, Werb Zena, Matrix Metalloproteinases: Regulators of the Tumor Microenvironment, 10.1016/j.cell.2010.03.015
  6. Matrix Metalloproteinases and Endometriosis, 10.1055/s-2003-41322
  7. Nuttall Robert K, Sampieri Clara L, Pennington Caroline J, Gill Sean E, Schultz Gilbert A, Edwards Dylan R, Expression analysis of the entire MMP and TIMP gene families during mouse tissue development, 10.1016/s0014-5793(04)00281-9
  8. Bar-Or A., Analyses of all matrix metalloproteinase members in leukocytes emphasize monocytes as major inflammatory mediators in multiple sclerosis, 10.1093/brain/awg285
  9. BERNAL FABIÁN, HARTUNG HANS-PETER, KIESEIER BERND C, Tissue mRNA expression in rat of newly described matrix metalloproteinases, 10.4067/s0716-97602005000200016
  10. Gaide Chevronnay Héloïse P., Galant Christine, Lemoine Pascale, Courtoy Pierre J., Marbaix Etienne, Henriet Patrick, Spatiotemporal Coupling of Focal Extracellular Matrix Degradation and Reconstruction in the Menstrual Human Endometrium, 10.1210/en.2009-0750
  11. Hagemann T., Wilson J., Burke F., Kulbe H., Li N. F., Pluddemann A., Charles K., Gordon S., Balkwill F. R., Ovarian Cancer Cells Polarize Macrophages Toward A Tumor-Associated Phenotype, 10.4049/jimmunol.176.8.5023
  12. Kevorkian Lara, Young David A., Darrah Clare, Donell Simon T., Shepstone Lee, Porter Sarah, Brockbank Sarah M. V., Edwards Dylan R., Parker Andrew E., Clark Ian M., Expression profiling of metalloproteinases and their inhibitors in cartilage, 10.1002/art.11433
  13. Lamblin Nicolas, Ratajczak Philippe, Hot David, Dubois Emilie, Chwastyniak Maggy, Beseme Olivia, Drobecq Hervé, Lemoine Yves, Koussa Mohammad, Amouyel Philippe, Pinet Florence, Profile of Macrophages in Human Abdominal Aortic Aneurysms: A Transcriptomic, Proteomic, and Antibody Protein Array Study, 10.1021/pr100250s
  14. Hegedüs Luca, Cho Hyojin, Xie Xian, Eliceiri George L., Additional MDA-MB-231 breast cancer cell matrix metalloproteinases promote invasiveness, 10.1002/jcp.21417
  15. Köhrmann Andrea, Kammerer Ulrike, Kapp Michaela, Dietl Johannes, Anacker Jelena, Expression of matrix metalloproteinases (MMPs) in primary human breast cancer and breast cancer cell lines: New findings and review of the literature, 10.1186/1471-2407-9-188
  16. Viklund Håkan, Bernsel Andreas, Skwark Marcin, Elofsson Arne, SPOCTOPUS: a combined predictor of signal peptides and membrane protein topology, 10.1093/bioinformatics/btn550
  17. Pelham Hugh R.B., The retention signal for soluble proteins of the endoplasmic reticulum, 10.1016/0968-0004(90)90303-s
  18. Lynes Emily M., Simmen Thomas, Urban planning of the endoplasmic reticulum (ER): How diverse mechanisms segregate the many functions of the ER, 10.1016/j.bbamcr.2011.06.011
  19. Krijnse-Locker J., Parton R. G., Fuller S. D., Griffiths G., Dotti C. G., The organization of the endoplasmic reticulum and the intermediate compartment in cultured rat hippocampal neurons., 10.1091/mbc.6.10.1315
  20. Klausner R. D., Brefeldin A: insights into the control of membrane traffic and organelle structure, 10.1083/jcb.116.5.1071
  21. Miller Sven, Sparacio Sandra, Bartenschlager Ralf, Subcellular Localization and Membrane Topology of the Dengue Virus Type 2 Non-structural Protein 4B, 10.1074/jbc.m512697200
  22. Bordier, J Biol Chem, 256, 1604 (1981)
  23. DICKERSON H. W., CLARK T. G., FINDLY R. C., Ichthyophthirius multifiliis Has Membrane-Associated Immobilization Antigens, 10.1111/j.1550-7408.1989.tb01065.x
  24. Szczesna-Skorupa E., Browne N., Mead D., Kemper B., Positive charges at the NH2 terminus convert the membrane-anchor signal peptide of cytochrome P-450 to a secretory signal peptide., 10.1073/pnas.85.3.738
  25. Osenkowski Pamela, Toth Marta, Fridman Rafael, Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP), 10.1002/jcp.20064
  26. Tusnady G. E., Simon I., The HMMTOP transmembrane topology prediction server, 10.1093/bioinformatics/17.9.849
  27. Sprong Hein, van der Sluijs Peter, van Meer Gerrit, How proteins move lipids and lipids move proteins, 10.1038/35080071
  28. Ronchi Paolo, Colombo Sara, Francolini Maura, Borgese Nica, Transmembrane domain–dependent partitioning of membrane proteins within the endoplasmic reticulum, 10.1083/jcb.200710093
  29. Stornaiuolo M., KDEL and KKXX Retrieval Signals Appended to the Same Reporter Protein Determine Different Trafficking between Endoplasmic Reticulum, Intermediate Compartment, and Golgi Complex, 10.1091/mbc.e02-08-0468
  31. Alberini Cristina M., Bet Paola, Milstein Cesar, Sitia Roberto, Secretion of immunoglobulin M assembly intermediates in the presence of reducing agents, 10.1038/347485a0
  32. Anelli T., Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44, 10.1093/emboj/cdg491
  33. Wang Yu, Lam Karen S. L., Yau Ming-hon, Xu Aimin, Post-translational modifications of adiponectin: mechanisms and functional implications, 10.1042/bj20071492
  34. Nina Mafalda, Bernèche Simon, Roux Benoît, Anchoring of a monotopic membrane protein: the binding of prostaglandin H2 synthase-1 to the surface of a phospholipid bilayer, 10.1007/pl00006649
  35. Li Yi, Smith Tim, Grabski Sharon, DeWitt David L., The Membrane Association Sequences of the Prostaglandin Endoperoxide Synthases-1 and -2 Isozymes, 10.1074/jbc.273.45.29830
  36. Fowler Philip W., Coveney Peter V., A Computational Protocol for the Integration of the Monotopic Protein Prostaglandin H2 Synthase into a Phospholipid Bilayer, 10.1529/biophysj.105.077784
  37. Vander Heyden Abigail B, Naismith Teresa V, Snapp Erik L, Hanson Phyllis I, Static retention of the lumenal monotopic membrane protein torsinA in the endoplasmic reticulum : ER retention of monotopic membrane proteins, 10.1038/emboj.2011.233
  38. London Erwin, Shahidullah Khurshida, Transmembrane vs. non-transmembrane hydrophobic helix topography in model and natural membranes, 10.1016/
  39. Cauwe Bénédicte, Opdenakker Ghislain, Intracellular substrate cleavage: a novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases, 10.3109/10409238.2010.501783
  40. Pei Duanqing, Kang Tiebang, Qi Huaxiong, Cysteine Array Matrix Metalloproteinase (CA-MMP)/MMP-23 Is a Type II Transmembrane Matrix Metalloproteinase Regulated by a Single Cleavage for Both Secretion and Activation, 10.1074/jbc.m006493200
  41. Rangaraju Srikant, Khoo Keith K., Feng Zhi-Ping, Crossley George, Nugent Daniel, Khaytin Ilya, Chi Victor, Pham Cory, Calabresi Peter, Pennington Michael W., Norton Raymond S., Chandy K. George, Potassium Channel Modulation by a Toxin Domain in Matrix Metalloprotease 23, 10.1074/jbc.m109.071266
  42. Pei Duanqing, CA-MMP: a matrix metalloproteinase with a novel cysteine array, but without the classic cysteine switch, 10.1016/s0014-5793(99)01046-7
  43. Courtoy Pierre J., Analytical Subcellular Fractionation of Endosomal Compartments in Rat Hepatocytes, Subcellular Biochemistry (1993) ISBN:9781461363194 p.29-68, 10.1007/978-1-4615-3026-8_2
  44. Carpentier Sarah, N'Kuli Francisca, Grieco Giuseppina, Van Der Smissen Patrick, Janssens Virginie, Emonard Hervé, Bilanges Benoît, Vanhaesebroeck Bart, Gaide Chevronnay Héloïse P., Pierreux Christophe E., Tyteca Donatienne, Courtoy Pierre J., Class III Phosphoinositide 3-Kinase/VPS34 and Dynamin are Critical for Apical Endocytic Recycling : PI3K-III/VPS34 and Dynamin in Apical Endocytic Recycling, 10.1111/tra.12079
  45. Tahay Gaëlle, Wiame Elsa, Tyteca Donatienne, Courtoy Pierre J., Van Schaftingen Emile, Determinants of the enzymatic activity and the subcellular localization of aspartate N-acetyltransferase, 10.1042/bj20111179