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Science 24 August 1990:
Vol. 249. no. 4971, pp. 915 - 918
DOI: 10.1126/science.2392682
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Articles

Science, Vol 249, Issue 4971, 915-918
Copyright © 1990 by American Association for the Advancement of Science

articles

A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation

JC Loftus, TE O'Toole, EF Plow, A Glass, AL Frelinger 3rd, and MH Ginsberg

Committee on Vascular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.

The ligand-binding function of integrin adhesion receptors depends on divalent cations. A mutant alpha IIb beta 3 integrin (platelet gpIIb/IIIa) that lacks ligand recognition shows immunologic evidence of a perturbed interaction with divalent cations. This was found to be caused by a G----T mutation that resulted in an Asp119----Tyr119 substitution in the beta 3 subunit. This residue is proximal to bound ligand and is in a conserved region among integrins that are enriched in oxygenated residues. The spacing of these residues aligns with the calcium-binding residues in EF hand proteins, suggesting interaction with receptor-bound divalent cation as a mechanism of ligand binding common to all integrins.


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Defining Extracellular Integrin alpha -Chain Sites That Affect Cell Adhesion and Adhesion Strengthening without Altering Soluble Ligand Binding.
C. Pujades, R. Alon, R. L. Yauch, A. Masumoto, L. C. Burkly, C. Chen, T. A. Springer, R. R. Lobb, and M. E. Hemler (1997)
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K. O. Simon, E. M. Nutt, D. G. Abraham, G. A. Rodan, and L. T. Duong (1997)
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Blood 90, 3082-3088
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Effect of Ca2+ on GP IIb-IIIa Interactions With Integrilin : Enhanced GP IIb-IIIa Binding and Inhibition of Platelet Aggregation by Reductions in the Concentration of Ionized Calcium in Plasma Anticoagulated With Citrate.
D. R. Phillips, W. Teng, A. Arfsten, L. Nannizzi-Alaimo, M. M. White, C. Longhurst, S. J. Shattil, A. Randolph, J. A. Jakubowski, L. K. Jennings, et al. (1997)
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An RGD to LDV Motif Conversion within the Disintegrin Kistrin Generates an Integrin Antagonist That Retains Potency but Exhibits Altered Receptor Specificity. EVIDENCE FOR A FUNCTIONAL EQUIVALENCE OF ACIDIC INTEGRIN-BINDING MOTIFS.
V. H. Tselepis, L. J. Green, and M. J. Humphries (1997)
J. Biol. Chem. 272, 21341-21348
   Abstract »    Full Text »    PDF »
Molecular evolution of integrins: Genes encoding integrin beta  subunits from a coral and a sponge.
D. L. Brower, S. M. Brower, D. C. Hayward, and E. E. Ball (1997)
PNAS 94, 9182-9187
   Abstract »    Full Text »    PDF »
Changing Ligand Specificities of alpha vbeta 1 and alpha vbeta 3 Integrins by Swapping a Short Diverse Sequence of the beta  Subunit.
J. Takagi, T. Kamata, J. Meredith, W. Puzon-McLaughlin, and Y. Takada (1997)
J. Biol. Chem. 272, 19794-19800
   Abstract »    Full Text »    PDF »
A Three Amino Acid Deletion in Glycoprotein IIIa Is Responsible for Type I Glanzmann's Thrombasthenia: Importance of Residues Ile325Pro326Gly327 for beta 3 Integrin Subunit Association.
M.-C. Morel-Kopp, C. Kaplan, V. Proulle, V. Jallu, C. Melchior, O. Peyruchaud, M.-H. Aurousseau, and N. Kieffer (1997)
Blood 90, 669-677
   Abstract »    Full Text »    PDF »
Evidence That the Integrin beta 3 and beta 5 Subunits Contain a Metal Ion-dependent Adhesion Site-like Motif but Lack an I Domain.
E. C. K. Lin, B. I. Ratnikov, P. M. Tsai, E. R. Gonzalez, S. McDonald, A. J. Pelletier, and J. W. Smith (1997)
J. Biol. Chem. 272, 14236-14243
   Abstract »    Full Text »    PDF »
A Novel Peptide Motif for Platelet Fibrinogen Receptor Recognition.
J. Katada, Y. Hayashi, Y. Sato, M. Muramatsu, Y. Takiguchi, T. Harada, T. Fujiyoshi, and I. Uno (1997)
J. Biol. Chem. 272, 7720-7726
   Abstract »    Full Text »    PDF »
Epitopes of adhesion-perturbing monoclonal antibodies map within a predicted alpha-helical domain of the integrin beta 1 subunit.
D. Shih, D Boettiger, and C. Buck (1997)
J. Cell Sci. 110, 2619-2628
   Abstract »    PDF »
Inducible Tyrosine Phosphorylation of the beta 3 Integrin Requires the alpha v Integrin Cytoplasmic Tail.
S. D. Blystone, F. P. Lindberg, M. P. Williams, K. P. McHugh, and E. J. Brown (1996)
J. Biol. Chem. 271, 31458-31462
   Abstract »    Full Text »    PDF »
A Novel Activating Anti-beta 1 Integrin Monoclonal Antibody Binds to the Cysteine-rich Repeats in the beta 1 Chain.
R. J. Faull, J. Wang, D. I. Leavesley, W. Puzon, G. R. Russ, D. Vestweber, and Y. Takada (1996)
J. Biol. Chem. 271, 25099-25106
   Abstract »    Full Text »    PDF »
Identifying the Putative Metal Ion-dependent Adhesion Site in the beta 2 (CD18) Subunit Required for alpha Lbeta 2 and alpha Mbeta 2 Ligand Interactions.
T. G. Goodman and M. L. Bajt (1996)
J. Biol. Chem. 271, 23729-23736
   Abstract »    Full Text »    PDF »
A Region of the Yersinia pseudotuberculosis Invasin Protein That Contributes to High Affinity Binding to Integrin Receptors.
L. H. Saltman, Y. Lu, E. M. Zaharias, and R. R. Isberg (1996)
J. Biol. Chem. 271, 23438-23444
   Abstract »    Full Text »    PDF »
An Allosteric Ca2+ Binding Site on the beta3-Integrins That Regulates the Dissociation Rate for RGD Ligands.
D. D. Hu, C. F. Barbas III, and J. W. Smith (1996)
J. Biol. Chem. 271, 21745-21751
   Abstract »    Full Text »    PDF »
Ligand Binding to Integrin alpha IIbbeta 3 Is Dependent on a MIDAS-like Domain in the beta 3 Subunit.
E. C. Tozer, R. C. Liddington, M. J. Sutcliffe, A. H. Smeeton, and J. C. Loftus (1996)
J. Biol. Chem. 271, 21978-21984
   Abstract »    Full Text »    PDF »
A Molecular Basis for Affinity Modulation of Fab Ligand Binding to Integrin alpha IIbbeta 3.
T. J. Kunicki, D. S. Annis, Y.-J. Deng, J. C. Loftus, and S. J. Shattil (1996)
J. Biol. Chem. 271, 20315-20321
   Abstract »    Full Text »    PDF »
Critical Residues for Ligand Binding in an I Domain-like Structure of the Integrin beta 1 Subunit.
W. Puzon-McLaughlin and Y. Takada (1996)
J. Biol. Chem. 271, 20438-20443
   Abstract »    Full Text »    PDF »
Critical Residues of Integrin alpha IIb Subunit for Binding of alpha IIbbeta 3 (Glycoprotein IIb-IIIa) to Fibrinogen and Ligand-mimetic Antibodies (PAC-1, OP-G2, and LJ-CP3).
T. Kamata, A. Irie, M. Tokuhira, and Y. Takada (1996)
J. Biol. Chem. 271, 18610-18615
   Abstract »    Full Text »    PDF »
The Ligand Recognition Specificity of beta(3) Integrins.
K. Suehiro, J. W. Smith, and E. F. Plow (1996)
J. Biol. Chem. 271, 10365-10371
   Abstract »    Full Text »    PDF »
Platelets and Coronary Artery Disease.
R. I. Handin (1996)
N. Engl. J. Med. 334, 1126-1128
   Full Text »
The Amino-terminal One-third of alpha[IMAGE] Defines the Ligand Recognition Specificity of Integrin alpha[IMAGE]beta(3).
J. C. Loftus, C. E. Halloran, M. H. Ginsberg, L. P. Feigen, J. A. Zablocki, and J. W. Smith (1996)
J. Biol. Chem. 271, 2033-2039
   Abstract »    Full Text »    PDF »
Getting integrins into shape: recent insights into how integrin activity is regulated by conformational changes.
A. Mould (1996)
J. Cell Sci. 109, 2613-2618
   PDF »
{alpha}vß3 Integrin Expression in Normal and Atherosclerotic Artery.
M. Hoshiga, C. E. Alpers, L. L. Smith, C. M. Giachelli, and S. M. Schwartz (1995)
Circ. Res. 77, 1129-1135
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Regulation of Integrin alpha5beta1-Fibronectin Interactions by Divalent Cations.
A. P. Mould, S. K. Akiyama, and M. J. Humphries (1995)
J. Biol. Chem. 270, 26270-26277
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Distinct Ligand Binding Sites in the I Domain of Integrin alpha(M)beta(2) That Differentially Affect a Divalent Cation-dependent Conformation.
S. L. McGuire and M. L. Bajt (1995)
J. Biol. Chem. 270, 25866-25871
   Abstract »    Full Text »    PDF »
Topography of Ligand-induced Binding Sites, Including a Novel Cation-sensitive Epitope (AP5) at the Amino Terminus, of the Human Integrin [IMAGE][IMAGE] Subunit.
S. Honda, Y. Tomiyama, A. J. Pelletier, D. Annis, Y. Honda, R. Orchekowski, Z. Ruggeri, and T. J. Kunicki (1995)
J. Biol. Chem. 270, 11947-11954
   Abstract »    Full Text »    PDF »
Mutation of the Cytoplasmic Domain of the Integrin [IMAGE][IMAGE]Subunit.
J. Ylänne, J. Huuskonen, T. E. O'Toole, M. H. Ginsberg, I. Virtanen, and C. G. Gahmberg (1995)
J. Biol. Chem. 270, 9550-9557
   Abstract »    Full Text »    PDF »
Crystal Structure of the OPG2 Fab.
R. Kodandapani, B. Veerapandian, T. J. Kunicki, and K. R. Ely (1995)
J. Biol. Chem. 270, 2268-2273
   Abstract »    Full Text »    PDF »
Involvement of alpha(v)beta(3) Integrin in Mediating Fibrin Gel Retraction.
Y. Katagiri, T. Hiroyama, N. Akamatsu, H. Suzuki, H. Yamazaki, and K. Tanoue (1995)
J. Biol. Chem. 270, 1785-1790
   Abstract »    Full Text »    PDF »
Integrin signaling: roles for the cytoplasmic tails of alpha IIb beta 3 in the tyrosine phosphorylation of pp125FAK.
L Leong, P. Hughes, M. Schwartz, M. Ginsberg, and S. Shattil (1995)
J. Cell Sci. 108, 3817-3825
   Abstract »    PDF »
beta(2)(CD18) Mutations Abolish Ligand Recognition by I Domain Integrins LFA-1 (alpha(L)beta(2), CD11a/CD18) and MAC-1 (alpha(M)beta(2), CD11b/CD18).
M. L. Bajt, T. Goodman, and S. L. McGuire (1995)
J. Biol. Chem. 270, 94-98
   Abstract »    Full Text »    PDF »
Role of integrins in melanocyte attachment and dendricity.
M Hara, M Yaar, A Tang, M. Eller, W Reenstra, and B. Gilchrest (1994)
J. Cell Sci. 107, 2739-2748
   Abstract »    PDF »
Functional down-regulation of alpha 5 beta 1 integrin in keratinocytes is reversible but commitment to terminal differentiation is not.
N. Hotchin, N. Kovach, and F. Watt (1993)
J. Cell Sci. 106, 1131-1138
   Abstract »    PDF »
A novel, tissue-specific integrin subunit, beta nu, expressed in the midgut of Drosophila melanogaster.
G. Yee and R. Hynes (1993)
Development 118, 845-858
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Effects of polystyrene surface chemistry on the biological activity of solid phase fibronectin and vitronectin, analysed with monoclonal antibodies.
P. Underwood, J. Steele, and B. Dalton (1993)
J. Cell Sci. 104, 793-803
   Abstract »    PDF »
Ligand Binding to Integrins: Dynamic Regulation and Common Mechanisms.
M.H. Ginsberg, T.E. O'Toole, J.C. Loftus, and E.F. Plow (1992)
Cold Spring Harb Symp Quant Biol 57, 221-231
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The Role of alpha and beta Chains in Ligand Recognition by beta 7 Integrins.
J. M. G. Higgins, M. Cernadas, K. Tan, A. Irie, J.-h. Wang, Y. Takada, and M. B. Brenner (2000)
J. Biol. Chem. 275, 25652-25664
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The Top of the Inserted-like Domain of the Integrin Lymphocyte Function-associated Antigen-1 beta Subunit Contacts the alpha Subunit beta -Propeller Domain near beta -Sheet 3.
Q. Zang, C. Lu, C. Huang, J. Takagi, and T. A. Springer (2000)
J. Biol. Chem. 275, 22202-22212
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Urokinase-type Plasminogen Activator Receptor (CD87) Is a Ligand for Integrins and Mediates Cell-Cell Interaction.
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Ligand Binding to Integrins.
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