Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin

Cell. 1986 Jul 18;46(2):271-82. doi: 10.1016/0092-8674(86)90744-0.


We describe the isolation, characterization, and sequence of cDNA clones encoding one subunit of the complex of membrane glycoproteins that forms part of the transmembrane connection between the extracellular matrix and the cytoskeleton. The cDNA sequence encodes a polypeptide of 89 kd that has features strongly suggesting the presence of a large N-terminal extracellular domain, a single transmembrane segment, and a small C-terminal cytoplasmic domain. The extracellular domain contains a threefold repeat of a novel 40 residue cysteine-rich segment, and the cytoplasmic domain contains a tyrosine residue that is a potential site for phosphorylation by tyrosine kinases. We propose the name integrin for this protein complex to denote its role as an integral membrane complex involved in the transmembrane association between the extracellular matrix and the cytoskeleton.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Actins / metabolism*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Chick Embryo
  • Cloning, Molecular
  • Cytoskeleton / metabolism
  • DNA / isolation & purification
  • Extracellular Matrix / metabolism
  • Fibroblasts / metabolism
  • Fibronectins / metabolism*
  • Glycoproteins / isolation & purification*
  • Glycoproteins / metabolism
  • Integrins
  • Membrane Proteins / isolation & purification*
  • Membrane Proteins / metabolism


  • Actins
  • Fibronectins
  • Glycoproteins
  • Integrins
  • Membrane Proteins
  • DNA

Associated data

  • GENBANK/M14049