Open AccessAIM1 , a novel non-lens member of the βγ-crystallin superfamily, is associated with the control of tumorigenicity in human malignant melanoma
Author(s) -
Michael E. Ray,
Graeme Wistow,
Yan Su,
Paul S. Meltzer,
Jeffrey M. Trent
Publication year - 1997
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.94.7.3229
Subject(s) - biology , crystallin , gene , ras superfamily , genetics , intron , immunoglobulin superfamily , peptide sequence , homology (biology) , gene product , gene expression , biochemistry , gtp' , enzyme
AIM1 is a novel gene whose expression is associated with the experimental reversal of tumorigenicity of human malignant melanoma. The predicted protein product of the major 4.1-kb transcript shows striking similarity to the βγ-crystallin superfamily. All known members of this superfamily contain two or four characteristic motifs arranged as one or two symmetrical domains.AIM1 , in contrast, contains 12 βγ motifs, suggesting a 6-domain structure resembling a trimer of β- or γ-crystallin subunits. The structure of theAIM1 gene shows remarkable similarity to β-crystallin genes, with homologous introns delineating equivalent protein structural units. AIM1 is the first mammalian member of the βγ superfamily with a primarily non-lens role. Other parts of the predicted AIM1 protein sequence have weak similarity with filament or actin-binding proteins. AIM1 is a good candidate for the putative suppressor of malignant melanoma on chromosome 6, possibly exerting its effects through interactions with the cytoskeleton.