Formation of microvilli and phosphorylation of ERM family proteins by CD43, a potent inhibitor for cell adhesion: Cell detachment is a potential cue for ERM phosphorylation and organization of cell morphology

Cell Adhesion and Migration

Volumn 5, Issue 2, 2011, Pages 119-132

  Yamane, Junko ^a,c   Ohnishi, Hiroe ^a   Sasaki, Hiroyuki ^b   Narimatsu, Hisashi ^a   Ohgushi, Hajime ^a   Tachibana, Kouichi ^a  

^a NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^b JIKEI UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

Author keywords

CD43; Cell adhesion; Cell rounding; ERM; Integrin; Microvilli; Mucin; Phosphorylation

Indexed keywords

EZRIN; LEUKOSIALIN; MOESIN; RADIXIN;

ARTICLE; CELL ADHESION; CELL STRAIN HEK293; CELL STRUCTURE; CELL SURFACE; HUMAN; MICROVILLUS; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN MODIFICATION; PROTEIN PHOSPHORYLATION;

EID: 79952323609     PISSN: 19336918     EISSN: 19336926     Source Type: Journal    
DOI: 10.4161/cam.5.2.13908     Document Type: Article

References (46)

1. Tadokoro S, Shattil SJ, Eto K, Tai V, Liddington RC, de Pereda JM, et al. Talin binding to integrin β tails: a final common step in integrin activation. Science 2003; 302:103-6. (Pubitemid 37210697)
2. Moser M, Legate KR, Zent R, Fässler R. The tail of integrins, talin and kindlins. Science 2009; 324:895-9.
3. Askari JA, Buckley PA, Mould AP, Humphries MJ. Linking integrin conformation to function. J Cell Sci 2009; 122:165-70.
4. Carlsson SR, Fukuda M. Isolation and characterization of Leukosialin, a major sialoglycoprotein on human leukocytes. J Biol Chem 1986; 261:12779-86. (Pubitemid 17204241)
5. Rosenstein Y, Santana A, Pedraza-Alva G. CD43, a molecule with multiple functions. Immunol Res 1999; 20:89-99.
6. Manjunath N, Johnson RS, Staunton DE, Pasqualini R, Ardman B. Targeted disruption of CD43 gene enhances T lymphocyte adhesion. J Immunol 1993; 151:1528-34. (Pubitemid 23219291)
7. Manjunath N, Correa M, Ardman M, Ardman B. Negative regulation of T-cell adhesion and activation by CD43. Nature 1995; 377:535-8.
8. Ardman B, Sikorski MA, Staunton DE. CD43 interferes with T-lymphocyte adhesion. Proc Natl Acad Sci USA 1992; 89:5001-5.
9. Stockton BM, Cheng G, Manjunath N, Ardman B, von Andrian UH. Negative regulation of T cell homing by CD43. Immunity 1998; 8:373-81. (Pubitemid 28188897)
10. Drew E, Merzaban JS, Seo W, Ziltener HJ, McNagny KM. CD34 and CD43 inhibit mast cell adhesion and are required for optimal mast cell reconstitution. Immunity 2005; 22:43-57. (Pubitemid 40143450)
11. del Pozo MA, Sánchez-Mateos P, Nieto M, Sánchez-Madrid F. Chemokines regulate cellular polarization and adhesion receptor redistribution during lymphocyte interaction with endothelium and extracellular matrix. Involvement of camp signaling pathway. J Cell Biol 1995; 131:495-508.
12. Sánchez-Madrid F, del Pozo MA. Leukocyte polarization in cell migration and immune interaction. EMBO J 1999; 18:501-11. (Pubitemid 29057235)
13. Soler M, Merant C, Servant C, Fraterno M, Allasia C, Lissitzky JC, et al. Leukosialin (CD43) behavior during adhesion of human monocytic THP-1 cells to red blood cells. J Leukoc Biol 1997; 61:609-18. (Pubitemid 27234458)
14. Shaw AS. Ferming up the synapse. Immunity 2001; 15:683-6. (Pubitemid 34008497)
15. Pallant A, Eskenazi A, Mattei MG, Fournier RE, Carlsson SR, Fukuda M, et al. Characterization of cDNAs encoding human leukosialin and localization of the leukosialin gene to chromosome 16. Proc Natl Acad Sci USA 1989; 86:1328-32. (Pubitemid 19061539)
16. Fukuda M, Tsuboi S. Mucin-type O-glycans and leukosialin. Biochem Biophys Acta 1999; 1455:205-17.
17. Cyster JG, Shotton DM, Williams AF. The dimensions of the T lymphocyte glycoprotein leukosialin and identification of linear protein epitopes that can be modified by glycosylation. EMBO J 1991; 10:893-902. (Pubitemid 21905547)
18. Mooseker MS, Tilney LG. Organization of an actin filament-membrane complex: Filament polarity and membrane attachment in the microvilli of intestinal epithelial cells. J Cell Biol 1975; 67:725-43.
19. Chhabra ES, Higgs HN. The many faces of actin: matching assembly factors with cellular structures. Nat Cell Biol 2007; 9:1110-21. (Pubitemid 47500485)
20. van Ewijk W, Brons NH, Rozing J. Scanning Electron Microscopy of Homing and Recirculating Lymphocyte Populations. Cell Immunol 1975; 19:245-61.
21. Anderson AO, Anderson ND. Lymphocyte emigration from high endothelial venules in rat lymph nodes. Immunology 1976; 31:731-48.
22. von Andrian UH, Hasslen SR, Nelson RD, Erlandsen SL, Butcher EC. A central role for microvillous receptor presentation in leukocyte adhesion under flow. Cell 1995; 82:989-99.
23. Majstoravich S, Zhang J, Nicholson-Dykstra S, Linder S, Friedrich W, Siminovitch KA, et al. Lymphocyte microvilli are dynamic, actin-dependent structures that do not require Wiskott-Aldrich syndrome protein (WASp) for their morphology. Blood 2004; 104:1396-403. (Pubitemid 39166517)
24. Berlin C, Bargatze RF, Campbell JJ, von Andrian UH, Szabo MC, Hasslen SR, et al. α4 integrins mediate lymphocyte attachment and rolling under physiologic flow. Cell 1995; 80:413-22.
25. Singer II, Scott S, Kawka DW, Chin J, Daugherty BL, DeMartino JA, et al. CCR5, CXCR4 and CD4 are clustered and closely apposed on microvilli of human macrophages and T cells. J Virol 2001; 75:3779-90. (Pubitemid 32246387)
26. Brown MJ, Nijhara R, Hallam JA, Gignac M, Yamada KM, Erlandsen SL, et al. Chemokine stimulation of human peripheral blood T lymphocytes induces rapid dephosphorylation of ERM proteins, which facilitates loss of microvilli and polarization. Blood 2003; 102:3890-9. (Pubitemid 37486967)
27. Ager A, Mistry S. Interaction between lymphocytes and cultured high endothelial cells: an in vitro model of lymphocyte migration across high endothelial venule endothelium. Eur J Immunol 1988; 18:1265-74.
28. Okumura S, Muraoka O, Tsukamoto Y, Tanaka H, Kohama K, Miki N, et al. Involvement of gicerin in the extension of microvilli. Exp Cell Res 2001; 271:269-76. (Pubitemid 33141208)
29. Guezguez B, Vigneron P, Lamerant N, Kieda C, Jaffredo T, Dunon D. Dual role of melanoma cell adhesion molecule (MCAM)/CD146 in lymphocyte endothelium interaction: MCAM/CD146 promotes rolling via microvilli induction in lymphocyte and is an endothelial adhesion receptor. J Immunol 2007; 179:6673-85.
30. Nielsen JS, Graves ML, Chelliah S, Vogl AW, Roskelley CD, McNagny KM. The CD34-related molecule Podocalyxin is a potent inducer of microvillous formation. PLoS One 2007; 2:e237.
31. Yonemura S, Nagafuchi A, Sato N, Tsukita S. Concentration of an integral membrane protein, CD43(leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletons. J Cell Biol 1993; 120:437-49. (Pubitemid 23040082)
32. Yonemura S, Tsukita S, Tsukita S. Direct involvement of Ezrin/Radixin/Moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins. J Cell Biol 1999; 145:1497-509. (Pubitemid 29310006)
33. Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S, et al. Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43 and ICAM-2. J Cell Biol 1998; 140:885-95. (Pubitemid 28141226)
34. Bretscher A. Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells. J Cell Biol 1983; 97:425-32.
35. Fiévet B, Louvard D, Arpin M. ERM proteins in epithelial cell organization and functions. Biochem Biophys Acta 2007; 1773:653-60. (Pubitemid 46660175)
36. Niggli V, Rossy J. Ezrin/radixin/moesin: versatile controllers of signaling molecules and of the cortical cytoskeleton. Int J Biochem Cell Biol 2008; 40:344-9. (Pubitemid 351241219)
37. Takeuchi K, Sato N, Kasahara H, Funayama N, Nagafuchi A, Yonemura S, et al. Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members. J Cell Biol 1994; 125:1371-84. (Pubitemid 24189539)
38. Pearson MA, Reczek D, Bretscher A, Karplus PA. Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell 2000; 101:259-70.
39. Hamada K, Shimizu T, Matsui T, Tsukita S, Tsukita S, Hakoshima T. Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. EMBO J 2000; 19:4449-62.
40. Li Q, Nance MR, Kulikauskas R, Nyberg K, Fehon R, Karplus PA, et al. Self-masking in an intact ERM-merlin protein: an active role for the central α-helical domain. J Mol Biol 2007; 365:1446-59. (Pubitemid 46055267)
41. Lee JH, Katakai T, Hara T, Gonda H, Sugai M, Shimizu A. Roles of p-ERM and Rho-ROCK signaling in lymphocyte polarity and uropod formation. J Cell Biol 2004; 167:327-37. (Pubitemid 39435075)
42. Kunda P, Pelling AE, Liu T, Baum B. Moesin controls cortical rigidity, cell rounding, and spindle morphogenesis during mitosis. Curr Biol 2008; 18:91-101.
43. Hao JJ, Liu Y, Kruhlak M, Debell KE, Rellahan BL, Shaw S. Phospholipase C-mediated hydrolysis of PIP2 releases ERM proteins from lymphocyte membrane. J Cell Biol 2009; 184:451-62.
44. Tsukita Sa, Oishi K, Sato N, Sagara J, Kawai A, Tsukita Sh. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. J Cell Biol 1994; 126:391-401. (Pubitemid 24226255)
45. Yonemura S, Matsui T, Tsukita S, Tsukita S. Rhodependent and -independent activation mechanisms of ezrin/radixin/moesin proteins: an essential role for polyphosphoinositides in vivo. J Cell Sci 2002; 115:2569-80. (Pubitemid 34778074)
46. Kamiguchi K, Tachibana K, Iwata S, Ohashi Y, Morimoto C. Cas-L is required for β1 integrin-mediated costimulation in human T cells. J Immunol 1999; 163:563-8. (Pubitemid 29328056)