Determination of the border between the transmembrane and cytoplasmic domains of human integrin subunits.
In this study we have determined the position of the C-terminal end of the transmembrane domains of human integrin subunits (alpha2, alpha5, beta1, beta2) in microsomal membranes using the glycosylation mapping technique. In contrast to the common view, the transmembrane helices were found to extend roughly to Phe(1129) in alpha2, to Phe(1026) in alpha5, to Ile(757) in beta1, and to His(728) in beta2. The alpha-carbon of the conserved lysine present near the C-terminal end of the transmembrane helix (Lys(1125) in alpha2, Lys(1022) in alpha5, Lys(752) in beta1, and Lys(724) in beta2) is buried in the plasma membrane, and the charged amino group most likely reaches into the polar head-group region of the lipid bilayer. A possible role for the conserved lysine in integrin function is discussed.
Armulik
A
A
Department of Medical Biochemistry, The Biomedical Center, Uppsala University, S-751 23, Uppsala, Sweden.
Nilsson
I
I
von Heijne
G
G
Johansson
S
S
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000737:chemistry; D017124:Conserved Sequence; D003593:Cytoplasm / Q000737:chemistry; D006031:Glycosylation; D006801:Humans; D016023:Integrins / Q000737:chemistry*; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary
D016023:Integrins