The integrins

Yoshikazu Takada, Xiaojing Ye, Scott Simon

Research output: Contribution to journalArticle

545 Citations (Scopus)

Abstract

The integrins are a superfamily of cell adhesion receptors that bind to extracellular matrix ligands, cell-surface ligands, and soluble ligands. They are transmembrane αβ heterodimers and at least 18 α and eight β subunits are known in humans, generating 24 heterodimers. Members of this family have been found in mammals, chicken and zebrafish, as well as lower eukaryotes, including sponges, the nematode Caenorhabditis elegans (two α and one β subunits, generating two integrins) and the fruitfly Drosophila melanogaster (five α and one β, generating five integrins). The α and β subunits have distinct domain structures, with extracellular domains from each subunit contributing to the ligand-binding site of the heterodimer. The sequence arginine-glycine-aspartic acid (RGD) was identified as a general integrin-binding motif, but individual integrins are also specific for particular protein ligands. Immunologically important integrin ligands are the intercellular adhesion molecules (ICAMs), immunoglobulin superfamily members present on inflamed endothelium and antigen-presenting cells. On ligand binding, integrins transduce signals into the cell interior; they can also receive intracellular signals that regulate their ligand-binding affinity. Here we provide a brief overview that concentrates mostly on the organization, structure and function of mammalian integrins, which have been more extensively studied than integrins in other organisms.

Original languageEnglish (US)
Article number215
JournalGenome Biology
Volume8
Issue number5
DOIs
StatePublished - Jun 1 2007

Fingerprint

integrins
Integrins
ligand
Ligands
adhesion
domain structure
aspartic acid
eukaryote
antigen-presenting cells
ligands
antigen
Caenorhabditis elegans
Cell Adhesion Molecules
sponge
Porifera
Zebrafish
Antigen-Presenting Cells
fruit flies
endothelium
Eukaryota

ASJC Scopus subject areas

  • Genetics
  • Cell Biology
  • Ecology, Evolution, Behavior and Systematics

Cite this

The integrins. / Takada, Yoshikazu; Ye, Xiaojing; Simon, Scott.

In: Genome Biology, Vol. 8, No. 5, 215, 01.06.2007.

Research output: Contribution to journalArticle

Takada, Y, Ye, X & Simon, S 2007, 'The integrins', Genome Biology, vol. 8, no. 5, 215. https://doi.org/10.1186/gb-2007-8-5-215
Takada, Yoshikazu ; Ye, Xiaojing ; Simon, Scott. / The integrins. In: Genome Biology. 2007 ; Vol. 8, No. 5.
@article{e1427bc74c4045d28160f29a24b4afa4,
title = "The integrins",
abstract = "The integrins are a superfamily of cell adhesion receptors that bind to extracellular matrix ligands, cell-surface ligands, and soluble ligands. They are transmembrane αβ heterodimers and at least 18 α and eight β subunits are known in humans, generating 24 heterodimers. Members of this family have been found in mammals, chicken and zebrafish, as well as lower eukaryotes, including sponges, the nematode Caenorhabditis elegans (two α and one β subunits, generating two integrins) and the fruitfly Drosophila melanogaster (five α and one β, generating five integrins). The α and β subunits have distinct domain structures, with extracellular domains from each subunit contributing to the ligand-binding site of the heterodimer. The sequence arginine-glycine-aspartic acid (RGD) was identified as a general integrin-binding motif, but individual integrins are also specific for particular protein ligands. Immunologically important integrin ligands are the intercellular adhesion molecules (ICAMs), immunoglobulin superfamily members present on inflamed endothelium and antigen-presenting cells. On ligand binding, integrins transduce signals into the cell interior; they can also receive intracellular signals that regulate their ligand-binding affinity. Here we provide a brief overview that concentrates mostly on the organization, structure and function of mammalian integrins, which have been more extensively studied than integrins in other organisms.",
author = "Yoshikazu Takada and Xiaojing Ye and Scott Simon",
year = "2007",
month = "6",
day = "1",
doi = "10.1186/gb-2007-8-5-215",
language = "English (US)",
volume = "8",
journal = "Genome Biology",
issn = "1465-6914",
publisher = "BioMed Central",
number = "5",

}

TY - JOUR

T1 - The integrins

AU - Takada, Yoshikazu

AU - Ye, Xiaojing

AU - Simon, Scott

PY - 2007/6/1

Y1 - 2007/6/1

N2 - The integrins are a superfamily of cell adhesion receptors that bind to extracellular matrix ligands, cell-surface ligands, and soluble ligands. They are transmembrane αβ heterodimers and at least 18 α and eight β subunits are known in humans, generating 24 heterodimers. Members of this family have been found in mammals, chicken and zebrafish, as well as lower eukaryotes, including sponges, the nematode Caenorhabditis elegans (two α and one β subunits, generating two integrins) and the fruitfly Drosophila melanogaster (five α and one β, generating five integrins). The α and β subunits have distinct domain structures, with extracellular domains from each subunit contributing to the ligand-binding site of the heterodimer. The sequence arginine-glycine-aspartic acid (RGD) was identified as a general integrin-binding motif, but individual integrins are also specific for particular protein ligands. Immunologically important integrin ligands are the intercellular adhesion molecules (ICAMs), immunoglobulin superfamily members present on inflamed endothelium and antigen-presenting cells. On ligand binding, integrins transduce signals into the cell interior; they can also receive intracellular signals that regulate their ligand-binding affinity. Here we provide a brief overview that concentrates mostly on the organization, structure and function of mammalian integrins, which have been more extensively studied than integrins in other organisms.

AB - The integrins are a superfamily of cell adhesion receptors that bind to extracellular matrix ligands, cell-surface ligands, and soluble ligands. They are transmembrane αβ heterodimers and at least 18 α and eight β subunits are known in humans, generating 24 heterodimers. Members of this family have been found in mammals, chicken and zebrafish, as well as lower eukaryotes, including sponges, the nematode Caenorhabditis elegans (two α and one β subunits, generating two integrins) and the fruitfly Drosophila melanogaster (five α and one β, generating five integrins). The α and β subunits have distinct domain structures, with extracellular domains from each subunit contributing to the ligand-binding site of the heterodimer. The sequence arginine-glycine-aspartic acid (RGD) was identified as a general integrin-binding motif, but individual integrins are also specific for particular protein ligands. Immunologically important integrin ligands are the intercellular adhesion molecules (ICAMs), immunoglobulin superfamily members present on inflamed endothelium and antigen-presenting cells. On ligand binding, integrins transduce signals into the cell interior; they can also receive intracellular signals that regulate their ligand-binding affinity. Here we provide a brief overview that concentrates mostly on the organization, structure and function of mammalian integrins, which have been more extensively studied than integrins in other organisms.

UR - http://www.scopus.com/inward/record.url?scp=34548826824&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34548826824&partnerID=8YFLogxK

U2 - 10.1186/gb-2007-8-5-215

DO - 10.1186/gb-2007-8-5-215

M3 - Article

VL - 8

JO - Genome Biology

JF - Genome Biology

SN - 1465-6914

IS - 5

M1 - 215

ER -