Structure and binding interface of the cytosolic tails of αxβ2 integrin

PLoS ONE

Volumn 7, Issue 7, 2012, Pages

  Chua, Geok Lin ^a   Tang, Xiao Yan ^a   Patra, Alok Tanala ^a   Tan, Suet Mien ^a   Bhattacharjya, Surajit ^a  

^a NANYANG TECHNOLOGICAL UNIVERSITY   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA INTEGRIN; ALPHA10BETA2 INTEGRIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; MICELLE; MOLECULAR DOCKING; MOLECULAR MODEL; NITROGEN NUCLEAR MAGNETIC RESONANCE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE;

AMINO ACID SEQUENCE; CYTOSOL; INTEGRIN ALPHAXBETA2; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MYRISTIC ACID; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN MODIFICATION, TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY;

EID: 84864857773     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0041924     Document Type: Article

References (37)

1. Giancotti FG, Ruoslahti E, ((1999)) Integrin signaling. Science 285:: 1028--1032.
2. Hynes RO, ((2002)) Integrins: bidirectional, allosteric signaling machines. Cell 110:: 673--687.
3. Tan SM, ((2012)) The leucocyte β2 (CD18) integrins: the structure, functional regulation and signalling properties. Bioscience reports 32:: 241--269.
4. Vorup-Jensen T, Carman CV, Shimaoka M, Schuck P, Svitel J, et al. ((2005)) Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin αXβ2. Proceedings of the National Academy of Sciences of the United States of America 102:: 1614--1619.
5. Wu H, Perrard XD, Wang Q, Perrard JL, Polsani VR, et al. ((2010)) CD11c expression in adipose tissue and blood and its role in diet-induced obesity. Arteriosclerosis, thrombosis, and vascular biology 30:: 186--192.
6. Wu H, Gower RM, Wang H, Perrard XY, Ma R, et al. ((2009)) Functional role of CD11c+ monocytes in atherogenesis associated with hypercholesterolemia. Circulation 119:: 2708--2717.
7. Keizer GD, Te Velde AA, Schwarting R, Figdor CG, De Vries JE, ((1987)) Role of p150,95 in adhesion, migration, chemotaxis and phagocytosis of human monocytes. European journal of immunology 17:: 1317--1322.
8. O'Doherty U, Peng M, Gezelter S, Swiggard WJ, Betjes M, et al. ((1994)) Human blood contains two subsets of dendritic cells, one immunologically mature and the other immature. Immunology 82:: 487--493.
9. Chan BM, Kassner PD, Schiro JA, Byers HR, Kupper TS, et al. ((1992)) Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains. Cell 68:: 1051--1060.
10. Kassner PD, Hemler ME, ((1993)) Interchangeable α chain cytoplasmic domains play a positive role in control of cell adhesion mediated by VLA-4, a β1 integrin. The Journal of experimental medicine 178:: 649--660.
11. Weber KS, Klickstein LB, Weber C, ((1999)) Specific activation of leukocyte β2 integrins lymphocyte function-associated antigen-1 and Mac-1 by chemokines mediated by distinct pathways via the α subunit cytoplasmic domains. Molecular biology of the cell 10:: 861--873.
12. Tang RH, Law SK, Tan SM, ((2006)) Selective recruitment of src family kinase Hck by leukocyte integrin αMβ2 but not αLβ2 or αXβ2. FEBS letters 580:: 4435--4442.
13. Bhunia A, Tang XY, Mohanram H, Tan SM, Bhattacharjya S, ((2009)) NMR solution conformations and interactions of integrin αLβ2 cytoplasmic tails. The Journal of biological chemistry 284:: 3873--3884.
14. Chua GL, Tang XY, Amalraj M, Tan SM, Bhattacharjya S, ((2011)) Structures and interaction analyses of integrin αMβ2 cytoplasmic tails. The Journal of biological chemistry 286:: 43842--43854.
15. Xie C, Zhu J, Chen X, Mi L, Nishida N, et al. ((2010)) Structure of an integrin with an αI domain, complement receptor type 4. The EMBO journal 29:: 666--679.
16. Vinogradova O, Haas TA, Plow EF, Qin J, ((2000)) A structual basis for integrin activation by the cytoplasmic tail of the αIIb subunit. Proceedings of the National Academy of Sciences of the United States of America 97:: 1450--1455.
17. Liu J, Jackson CW, Gruppo RA, Jennings LK, Gartner TK, ((2005)) The β3 subunit of the integrin αIIbβ3 regulates αIIb-mediated outside-in signaling. Blood 105:: 4345--4352.
18. Wishart DS, Sykes BD, ((1994)) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. Journal of biomolecular NMR 4:: 171--180.
19. Lyskov S, Gray JJ, ((2008)) The RosettaDock server for local protein-protein docking. Nucleic acids research 36:: W233--238.
20. Alahari SK, Reddig PJ, Juliano RL, ((2004)) The integrin-binding protein Nischarin regulates cell migration by inhibiting PAK. The EMBO journal 23:: 2777--2788.
21. Liu S, Thomas SM, Woodside DG, Rose DM, Kiosses WB, et al. ((1999)) Binding of paxillin to α4 integrins modifies integrin-dependent biological responses. Nature 402:: 676--681.
22. Naik UP, Patel PM, Parise LV, ((1997)) Identification of a novel calcium-binding protein that interacts with the integrin αIIb cytoplasmic domain. The Journal of biological chemistry 272:: 4651--4654.
23. Geng X, Tang RH, Law SK, Tan SM, ((2005)) Integrin CD11a cytoplasmic tail interacts with the CD45 membrane-proximal protein tyrosine phosphatase domain 1. Immunology 115:: 347--357.
24. Yin H, Slusky JS, Berger BW, Walters RS, Vilaire G, et al. ((2007)) Computational design of peptides that target transmembrane helices. Science 315:: 1817--1822.
25. Bernard E, Parthasarathi L, Cho MK, Aylward K, Raab M, et al. ((2009)) Ligand switching in cell-permeable peptides: manipulation of the α-integrin signature motif. ACS chemical biology 4:: 457--471.
26. Yang J, Ma Y-Q, Page RC, Misra S, Plow EF, et al. ((2009)) Structure of an integrin αIIbβ3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activtion. Proceedings of the National Academy of Sciences of the United States of America 42:: 17729--17734.
27. Lau T-L, Kim C, Ginsberg MH, Ulmer TS, ((2009)) The structure of the integrin αIIbβ3 transmembrane complex explains integrin transmembrane signalling. EMBO J 28:: 1351--1361.
28. Kim M, Carman CV, Springer TA, ((2003)) Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 301:: 1720--1725.
29. Hughes PE, Diaz-Gonzalez F, Leong L, Wu C, McDonald JA, et al. ((1996)) Breaking the integrin hinge. A defined structural constraint regulates integrin signaling. The Journal of biological chemistry 271:: 6571--6574.
30. Vallar L, Melchior C, Plancon S, Drobecq H, Lippens G, et al. ((1999)) Divalent cations differentially regulate integrin αIIb cytoplasmic tail binding to β3 and to calcium- and integrin-binding protein. The Journal of biological chemistry 274:: 17257--17266.
31. Vinogradova O, Velyvis A, Velyviene A, Hu B, Haas T, et al. ((2002)) A structural mechanism of integrin αIIbβ3 "inside-out" activation as regulated by its cytoplasmic face. Cell 110:: 587--597.
32. Ulmer TS, Yaspan B, Ginsberg MH, Campbell ID, ((2001)) NMR analysis of structure and dynamics of the cytosolic tails of integrin αIIbβ3 in aqueous solution. Biochemistry 40:: 7498--7508.
33. Li R, Babu CR, Lear JD, Wand AJ, Bennett JS, et al. ((2001)) Oligomerization of the integrin αIIbβ3: roles of the transmembrane and cytoplasmic domains. Proceedings of the National Academy of Sciences of the United States of America 98:: 12462--12467.
34. Metcalf DG, Moore DT, Wu Y, Kielec JM, Molnar K, et al. ((2010)) NMR analysis of the αIIbβ3 cytoplasmic inteactions suggest a mechanism for inetgrin regulation. Proceedings of the National Academy of Sciences of the United States of America 107:: 22481--22486.
35. Goddard TD, Kneller DGSPARKY. Graphical NMR Assignment and Integration program. University of California, San Francisco.
36. Guntert P, Mumenthaler C, Wuthrich K, ((1997)) Torsion angle dynamics for NMR structure calculation with the new program DYANA. Journal of molecular biology 273:: 283--298.
37. Laskowski RA, MacArthur MW, Moss DS, Thornton JM, ((1993)) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26:: 283--291.