Binding of the cytoplasmic domain of intercellular adhesion molecule-2 (ICAM-2) to alpha-actinin

被引:54
作者
Heiska, L
Kantor, C
Parr, T
Critchley, DR
Vilja, P
Gahmberg, CG
Carpen, O
机构
[1] UNIV HELSINKI,DEPT BIOSCI,DIV BIOCHEM,FIN-00014 HELSINKI,FINLAND
[2] UNIV LEICESTER,DEPT BIOCHEM,LEICESTER LE1 7RH,LEICS,ENGLAND
[3] UNIV TAMPERE,SCH MED,FIN-33101 TAMPERE,FINLAND
关键词
D O I
10.1074/jbc.271.42.26214
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Intercellular adhesion molecule-2 (ICAM-2) functions as a ligand for lymphocyte function-associated antigen-1 (LFA-1) and is involved in leukocyte adhesion, We studied intracellular associations of ICAM-2 using a peptide encompassing the cytoplasmic amino acids 231-254 as an affinity matrix, Among the proteins from placental lysates that bound to the peptide was alpha-actinin as demonstrated by immunoblotting. Purified, I-125-labeled alpha-actinin also bound to the peptide. Confocal microscopic analysis of Eahy926 cells demonstrated a colocalization of ICAM-2 and alpha-actinin. Of overlapping octapeptides covering the entire ICAM-2 cytoplasmic amino acids, ICAM-2(241-248) bound alpha-actinin most avidly and effectively competed with the longer cytoplasmic peptide for binding. The site of interaction in alpha-actinin was studied using bacterially expressed alpha-actinin fusion proteins, Several constructs covering nonoverlapping regions of alpha-actinin bound to the ICAM-2 cytoplasmic peptide suggesting that multiple regions in alpha-actinin can mediate the interaction, These results, together with previously demonstrated interactions between alpha-actinin and the adhesion proteins ICARS-1, L-selectin, beta(1)- and beta(2)-integrins emphasize the role of alpha-actinin as a linker between cell surface adhesion molecules and the actin containing cytoskeleton.
引用
收藏
页码:26214 / 26219
页数:6
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