Critical threonine and aspartic acid residues within the I domains of β2 integrins for interactions with intercellular adhesion molecule 1 (ICAM-1) and C3bi

T. Kamata, R. Wright, Yoshikazu Takada

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Abstract

Integrins mediate signal transduction through interactions with multiple cellular or extracellular matrix ligands. Evidence is accumulating that the I (or A) domain, a ~200-residue inserted sequence in some integrin α subunits, mediates ligand binding. We have previously shown that Thr-221 of the putative ligand binding sites within α2 I domain of α2β1 is critical for binding to collagen (Kamata, T., and Takada, Y. (1994) J. Biol. Chem. 269, 26006-26010). Here we report that the mutation of Thr-206 of αL blocks intercellular adhesion molecule 1 (ICAM-1) binding to αLβ2 and mutation of Thr-209 of αM blocks ICAM-1 and C3bi binding to αMβ2. The data indicate the Thr residues of αM and aL corresponding to Thr-221 of α2 are critically involved in the ligand interaction with β2 integrins. The mutations of the Asp-137 and Asp-239 of αL also block ICAM-1 binding to αLβ2, as do the corresponding Asp residues of α2 or αM in collagen/α2β1 or C3bi/αMβ2 interactions, respectively. These data suggest that these Thr and Asp residues, conserved among I domains, are critical for interaction with structurally distinct ligands (e.g. ICAMs, C3bi, and collagen).

Original languageEnglish (US)
Pages (from-to)12531-12535
Number of pages5
JournalJournal of Biological Chemistry
Volume270
Issue number21
DOIs
StatePublished - 1995
Externally publishedYes

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Complement C3b
Intercellular Adhesion Molecule-1
Threonine
Aspartic Acid
Integrins
Ligands
Collagen
Viperidae
Mutation
Signal transduction
Extracellular Matrix
Signal Transduction
Binding Sites

ASJC Scopus subject areas

  • Biochemistry

Cite this

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title = "Critical threonine and aspartic acid residues within the I domains of β2 integrins for interactions with intercellular adhesion molecule 1 (ICAM-1) and C3bi",
abstract = "Integrins mediate signal transduction through interactions with multiple cellular or extracellular matrix ligands. Evidence is accumulating that the I (or A) domain, a ~200-residue inserted sequence in some integrin α subunits, mediates ligand binding. We have previously shown that Thr-221 of the putative ligand binding sites within α2 I domain of α2β1 is critical for binding to collagen (Kamata, T., and Takada, Y. (1994) J. Biol. Chem. 269, 26006-26010). Here we report that the mutation of Thr-206 of αL blocks intercellular adhesion molecule 1 (ICAM-1) binding to αLβ2 and mutation of Thr-209 of αM blocks ICAM-1 and C3bi binding to αMβ2. The data indicate the Thr residues of αM and aL corresponding to Thr-221 of α2 are critically involved in the ligand interaction with β2 integrins. The mutations of the Asp-137 and Asp-239 of αL also block ICAM-1 binding to αLβ2, as do the corresponding Asp residues of α2 or αM in collagen/α2β1 or C3bi/αMβ2 interactions, respectively. These data suggest that these Thr and Asp residues, conserved among I domains, are critical for interaction with structurally distinct ligands (e.g. ICAMs, C3bi, and collagen).",
author = "T. Kamata and R. Wright and Yoshikazu Takada",
year = "1995",
doi = "10.1074/jbc.270.21.12531",
language = "English (US)",
volume = "270",
pages = "12531--12535",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
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T1 - Critical threonine and aspartic acid residues within the I domains of β2 integrins for interactions with intercellular adhesion molecule 1 (ICAM-1) and C3bi

AU - Kamata, T.

AU - Wright, R.

AU - Takada, Yoshikazu

PY - 1995

Y1 - 1995

N2 - Integrins mediate signal transduction through interactions with multiple cellular or extracellular matrix ligands. Evidence is accumulating that the I (or A) domain, a ~200-residue inserted sequence in some integrin α subunits, mediates ligand binding. We have previously shown that Thr-221 of the putative ligand binding sites within α2 I domain of α2β1 is critical for binding to collagen (Kamata, T., and Takada, Y. (1994) J. Biol. Chem. 269, 26006-26010). Here we report that the mutation of Thr-206 of αL blocks intercellular adhesion molecule 1 (ICAM-1) binding to αLβ2 and mutation of Thr-209 of αM blocks ICAM-1 and C3bi binding to αMβ2. The data indicate the Thr residues of αM and aL corresponding to Thr-221 of α2 are critically involved in the ligand interaction with β2 integrins. The mutations of the Asp-137 and Asp-239 of αL also block ICAM-1 binding to αLβ2, as do the corresponding Asp residues of α2 or αM in collagen/α2β1 or C3bi/αMβ2 interactions, respectively. These data suggest that these Thr and Asp residues, conserved among I domains, are critical for interaction with structurally distinct ligands (e.g. ICAMs, C3bi, and collagen).

AB - Integrins mediate signal transduction through interactions with multiple cellular or extracellular matrix ligands. Evidence is accumulating that the I (or A) domain, a ~200-residue inserted sequence in some integrin α subunits, mediates ligand binding. We have previously shown that Thr-221 of the putative ligand binding sites within α2 I domain of α2β1 is critical for binding to collagen (Kamata, T., and Takada, Y. (1994) J. Biol. Chem. 269, 26006-26010). Here we report that the mutation of Thr-206 of αL blocks intercellular adhesion molecule 1 (ICAM-1) binding to αLβ2 and mutation of Thr-209 of αM blocks ICAM-1 and C3bi binding to αMβ2. The data indicate the Thr residues of αM and aL corresponding to Thr-221 of α2 are critically involved in the ligand interaction with β2 integrins. The mutations of the Asp-137 and Asp-239 of αL also block ICAM-1 binding to αLβ2, as do the corresponding Asp residues of α2 or αM in collagen/α2β1 or C3bi/αMβ2 interactions, respectively. These data suggest that these Thr and Asp residues, conserved among I domains, are critical for interaction with structurally distinct ligands (e.g. ICAMs, C3bi, and collagen).

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