Association of Ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2)

Leena Heiska, Kaija Alfthan, Mikaela Grönholm, Pekka Vilja, Antti Vaheri, Olli Carpen

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

Ezrin is a cytoplasmic linker molecule between plasma membrane components and the actin-containing cytoskeleton.
We studied whether ezrin is associated with intercellular adhesion molecule (ICAM)-1, -2, and -3. In transfected cells, ICAM-1 and ICAM-2 colocalized with ezrin in microvillar projections, whereas an ICAM-1 construct attached to cell membrane via a glycophosphatidylinositol anchor was uniformly distributed on the cell surface.
An interaction of ICAM-2 and ezrin was seen by affinity precipitation, microtiter binding assay, coimmunoprecipitation, and surface plasmon resonance methods. The calculatedK D value was 3.3 × 10−7 M. Phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) induced an interaction of ezrin and ICAM-1 and enhanced the interaction of ezrin and ICAM-2, but ICAM-3 did not bind ezrin even in the presence of PtdIns(4,5)P2. PtdIns(4,5)P2 was shown to bind to cytoplasmic tails of ICAM-1 and ICAM-2, which are the first adhesion proteins demonstrated to interact with PtdIns(4,5)P2.
The results indicate an interaction of ezrin with ICAM-1 and ICAM-2 and suggest a regulatory role of phosphoinositide signaling pathways in regulation of ICAM-ezrin interaction.
Original languageEnglish
Pages (from-to)21893-21900
JournalJournal of Biological Chemistry
Volume273
Issue number34
DOIs
Publication statusPublished - 1998
MoE publication typeA1 Journal article-refereed

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Cell Adhesion Molecules
Intercellular Adhesion Molecule-1
Phosphatidylinositol 4,5-Diphosphate
Cell membranes
Phosphatidylinositols
Cell Membrane
ezrin
Surface Plasmon Resonance
Surface plasmon resonance
Anchors
Actin Cytoskeleton
Actins
Assays
Adhesion
Molecules

Cite this

Heiska, L., Alfthan, K., Grönholm, M., Vilja, P., Vaheri, A., & Carpen, O. (1998). Association of Ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Journal of Biological Chemistry, 273(34), 21893-21900. https://doi.org/10.1074/jbc.273.34.21893
Heiska, Leena ; Alfthan, Kaija ; Grönholm, Mikaela ; Vilja, Pekka ; Vaheri, Antti ; Carpen, Olli. / Association of Ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). In: Journal of Biological Chemistry. 1998 ; Vol. 273, No. 34. pp. 21893-21900.
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abstract = "Ezrin is a cytoplasmic linker molecule between plasma membrane components and the actin-containing cytoskeleton. We studied whether ezrin is associated with intercellular adhesion molecule (ICAM)-1, -2, and -3. In transfected cells, ICAM-1 and ICAM-2 colocalized with ezrin in microvillar projections, whereas an ICAM-1 construct attached to cell membrane via a glycophosphatidylinositol anchor was uniformly distributed on the cell surface. An interaction of ICAM-2 and ezrin was seen by affinity precipitation, microtiter binding assay, coimmunoprecipitation, and surface plasmon resonance methods. The calculatedK D value was 3.3 × 10−7 M. Phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) induced an interaction of ezrin and ICAM-1 and enhanced the interaction of ezrin and ICAM-2, but ICAM-3 did not bind ezrin even in the presence of PtdIns(4,5)P2. PtdIns(4,5)P2 was shown to bind to cytoplasmic tails of ICAM-1 and ICAM-2, which are the first adhesion proteins demonstrated to interact with PtdIns(4,5)P2. The results indicate an interaction of ezrin with ICAM-1 and ICAM-2 and suggest a regulatory role of phosphoinositide signaling pathways in regulation of ICAM-ezrin interaction.",
author = "Leena Heiska and Kaija Alfthan and Mikaela Gr{\"o}nholm and Pekka Vilja and Antti Vaheri and Olli Carpen",
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Heiska, L, Alfthan, K, Grönholm, M, Vilja, P, Vaheri, A & Carpen, O 1998, 'Association of Ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2)', Journal of Biological Chemistry, vol. 273, no. 34, pp. 21893-21900. https://doi.org/10.1074/jbc.273.34.21893

Association of Ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). / Heiska, Leena; Alfthan, Kaija; Grönholm, Mikaela; Vilja, Pekka; Vaheri, Antti; Carpen, Olli.

In: Journal of Biological Chemistry, Vol. 273, No. 34, 1998, p. 21893-21900.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Association of Ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2)

AU - Heiska, Leena

AU - Alfthan, Kaija

AU - Grönholm, Mikaela

AU - Vilja, Pekka

AU - Vaheri, Antti

AU - Carpen, Olli

PY - 1998

Y1 - 1998

N2 - Ezrin is a cytoplasmic linker molecule between plasma membrane components and the actin-containing cytoskeleton. We studied whether ezrin is associated with intercellular adhesion molecule (ICAM)-1, -2, and -3. In transfected cells, ICAM-1 and ICAM-2 colocalized with ezrin in microvillar projections, whereas an ICAM-1 construct attached to cell membrane via a glycophosphatidylinositol anchor was uniformly distributed on the cell surface. An interaction of ICAM-2 and ezrin was seen by affinity precipitation, microtiter binding assay, coimmunoprecipitation, and surface plasmon resonance methods. The calculatedK D value was 3.3 × 10−7 M. Phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) induced an interaction of ezrin and ICAM-1 and enhanced the interaction of ezrin and ICAM-2, but ICAM-3 did not bind ezrin even in the presence of PtdIns(4,5)P2. PtdIns(4,5)P2 was shown to bind to cytoplasmic tails of ICAM-1 and ICAM-2, which are the first adhesion proteins demonstrated to interact with PtdIns(4,5)P2. The results indicate an interaction of ezrin with ICAM-1 and ICAM-2 and suggest a regulatory role of phosphoinositide signaling pathways in regulation of ICAM-ezrin interaction.

AB - Ezrin is a cytoplasmic linker molecule between plasma membrane components and the actin-containing cytoskeleton. We studied whether ezrin is associated with intercellular adhesion molecule (ICAM)-1, -2, and -3. In transfected cells, ICAM-1 and ICAM-2 colocalized with ezrin in microvillar projections, whereas an ICAM-1 construct attached to cell membrane via a glycophosphatidylinositol anchor was uniformly distributed on the cell surface. An interaction of ICAM-2 and ezrin was seen by affinity precipitation, microtiter binding assay, coimmunoprecipitation, and surface plasmon resonance methods. The calculatedK D value was 3.3 × 10−7 M. Phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) induced an interaction of ezrin and ICAM-1 and enhanced the interaction of ezrin and ICAM-2, but ICAM-3 did not bind ezrin even in the presence of PtdIns(4,5)P2. PtdIns(4,5)P2 was shown to bind to cytoplasmic tails of ICAM-1 and ICAM-2, which are the first adhesion proteins demonstrated to interact with PtdIns(4,5)P2. The results indicate an interaction of ezrin with ICAM-1 and ICAM-2 and suggest a regulatory role of phosphoinositide signaling pathways in regulation of ICAM-ezrin interaction.

U2 - 10.1074/jbc.273.34.21893

DO - 10.1074/jbc.273.34.21893

M3 - Article

VL - 273

SP - 21893

EP - 21900

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 34

ER -