Intermediate monomer–dimer equilibrium structure of native ICAM-1: Implication for enhanced cell adhesion

Dimeric intercellular adhesion molecule-1 (ICAM-1) has been known to more efficiently mediate cell adhesion than monomeric ICAM-1. Here, we found that truncation of the intracellular domain of ICAM-1 significantly enhances surface dimerization based on the two criteria: 1) the binding degree of mono...

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Bibliographic Details
Published in:Experimental cell research 2011-01, Vol.317 (2), p.163-172
Main Authors: Oh, Hyun-Mee, Kwon, Min-Sung, Kim, Hyang-Jin, Jeon, Byeong-Hun, Kim, Hye-Ran, Choi, Hyang-Ok, Na, Bo-Ra, Eom, Soo-Hyun, Song, Nam Woong, Jun, Chang-Duk
Format: Article
Language:English
Subjects:
Amino Acid Substitution
Animals
Base Sequence
Cell adhesion
Cell adhesion & migration
Cell Adhesion - physiology
Cell Line
Cell Line, Transformed
Cercopithecus aethiops
CHO Cells
COS Cells
Cricetinae
Cricetulus
Dimer
Dimerization
DNA, Complementary
Endothelium, Vascular - cytology
Equilibrium
Humans
ICAM-1
Immunoglobulin superfamily
Intercellular Adhesion Molecule-1 - chemistry
Intercellular Adhesion Molecule-1 - genetics
Intercellular Adhesion Molecule-1 - metabolism
Intracellular domain
Jurkat Cells
Kidney - cytology
Macromolecular Substances - metabolism
Models, Structural
Molecular Sequence Data
Protein Structure, Tertiary - genetics
RNA, Small Interfering - metabolism
Transfection
Umbilical Veins - cytology
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Summary:Dimeric intercellular adhesion molecule-1 (ICAM-1) has been known to more efficiently mediate cell adhesion than monomeric ICAM-1. Here, we found that truncation of the intracellular domain of ICAM-1 significantly enhances surface dimerization based on the two criteria: 1) the binding degree of monomer-specific antibody CA-7 and 2) the ratio of dimer/monomer when a mutation (L42 → C42) was introduced in the interface of domain 1. Mutation analysis revealed that the positively charged amino acids, including very membrane-proximal 505R, are essential for maintaining the structural transition between the monomer and dimer. Despite a strong dimer presentation, the ICAM-1 mutants lacking an intracellular domain (IC1ΔCTD) or containing R to A substitution in position 505 ( 505R/A) supported a lower degree of cell adhesion than did wild-type ICAM-1. Collectively, these results demonstrate that the native structure of surface ICAM-1 is not a dimer, but is an intermediate monomer–dimer equilibrium structure by which the effectiveness of ICAM-1 can be fully achieved.
ISSN:0014-4827
1090-2422
DOI:10.1016/j.yexcr.2010.10.004