Beta 3-endonexin, a novel polypeptide that interacts specifically with the cytoplasmic tail of the integrin beta 3 subunit.
The adhesive and signaling functions of integrins are regulated through their cytoplasmic domains. We identified a novel 111 residue polypeptide, designated beta 3-endonexin, that interacted with the cytoplasmic tail of the beta 3 integrin subunit in a yeast two-hybrid system. This interaction is structurally specific, since it was reduced by ... 64% by a point mutation in the beta 3 cytoplasmic tail (S752-->P) that disrupts integrin signaling. Moreover, this interaction is integrin subunit specific since it was not observed with the cytoplasmic tails of the alpha IIb, beta 1, or beta 2 subunits. beta 3-Endonexin fusion proteins bound selectively to detergent-solubilized beta 3 from platelets and human umbilical vein endothelial cells, and beta 3-endonexin mRNA and protein were detected in platelets and other tissues. A related mRNA encoded a larger polypeptide that failed to bind to beta integrin tails. The apparent specificity of beta 3-endonexin for the beta 3 integrin subunit suggests potential mechanisms for selective modulation of integrin functions.
Mesh Terms:
Amino Acid Sequence, B-Lymphocytes, Base Sequence, Cloning, Molecular, Cytoplasm, Gene Expression, Humans, Integrins, Middle Aged, Molecular Sequence Data, Nuclear Proteins, Peptides, Proteins, RNA, Messenger, Sensitivity and Specificity
Amino Acid Sequence, B-Lymphocytes, Base Sequence, Cloning, Molecular, Cytoplasm, Gene Expression, Humans, Integrins, Middle Aged, Molecular Sequence Data, Nuclear Proteins, Peptides, Proteins, RNA, Messenger, Sensitivity and Specificity
J. Cell Biol.
Date: Nov. 01, 1995
PubMed ID: 7593198
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