ADD1:ADD3 binds DMTN

Stable Identifier
R-HSA-5226999
Type
Reaction [binding]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
Alpha-adducin (ADD1 aka ADDA) (Joshi et al. 1991) is a ubiquitously expressed, membrane-cytoskeletal protein that can promote the assembly of the spectrin-actin network. It is functional in a heterodimeric form, in complex with either a beta (ADD2 aka ADDB) (Khan et al. 2008) or a gamma (ADD3 aka ADDL) subunit (Citterio et al. 2003). Either complex is able to bind dematin (DMTN) (Azim et al. 1995), a membrane-cytoskeletal protein that can induce F-actin bundles formation and stabilization. It can also bind the erythrocyte membrane glucose transporter 1 (SLC2A1 aka GLUT1), and hence stabilise the spectrin-actin network to the erythrocytic plasma membrane (Khan et al. 2008).
Literature References
PubMed ID Title Journal Year
7615546 Isoform cloning, actin binding, and chromosomal localization of human erythroid dematin, a member of the villin superfamily

Azim, AC, Beggs, AH, Knoll, JH, Chishti, AH

J. Biol. Chem. 1995
18347014 Dematin and adducin provide a novel link between the spectrin cytoskeleton and human erythrocyte membrane by directly interacting with glucose transporter-1

Zeng, L, Khan, AA, Hanada, T, Mohseni, M, Chishti, AH, Jeong, JJ, Li, D, Reed, BC, Speicher, DW, Gaetani, M

J. Biol. Chem. 2008
1840603 Primary structure and domain organization of human alpha and beta adducin

Joshi, R, Otto, E, Gilligan, DM, McLaughlin, T, Bennett, V

J. Cell Biol. 1991
12951058 Expression analysis of the human adducin gene family and evidence of ADD2 beta4 multiple splicing variants

Bianchi, G, Catalano, M, Tizzoni, L, Citterio, L, Barlassina, C, Zerbini, G

Biochem. Biophys. Res. Commun. 2003
Participants
Participates
Orthologous Events
Authored
Reviewed
Created
Cite Us!