Association of the tetraspanin CD151 with the laminin-binding integrins alpha3beta1, alpha6beta1, alpha6beta4 and alpha7beta1 in cells in culture and in vivo.
CD151 is a cell surface protein that belongs to the tetraspanin superfamily. It forms complexes with the laminin-binding integrins alpha3beta1, alpha6beta1 and alpha6beta4 and is codistributed with these integrins in many tissues at sites of cell-matrix interactions. In this study we show that CD151 can also form stable complexes with the laminin-binding integrin alpha7beta1. The strength of this interaction is comparable to that between CD151 and alpha3beta1. Complexes of alpha3beta1, alpha6beta1 and alpha7beta1 with CD151 are equally well formed with all splice variants of the alpha3, alpha6 and alpha7 subunits, and complex formation is not affected by mutations that prevent the cleavage of the integrin alpha6 subunit. Like the expression of alpha3beta1 and alpha6beta1, expression of alpha7beta1 in K562 cells results in increased levels of CD151 at its surface. Two non-integrin laminin receptors, dystroglycan and the polypeptide on which the Lutheran blood group antigens are expressed, are also often colocalized with CD151, but no association with CD151-alpha3beta1 complexes was found with biochemical analysis. The anti-CD151 antibody TS151R detects an epitope at a site at which CD151 interacts with integrins, and therefore it cannot react with CD151 when it is bound to an integrin. Comparison of the straining patterns produced by TS151R with that by of an anti-CD151 antibody recognizing an epitope outside the binding site (P48) revealed that most tissues expressing one or more laminin-binding integrins reacted with P48 but not with TS151R. However, smooth muscle cells that express alpha7beta1 and renal tubular epithelial cells that express alpha6beta1 were stained equally well by TS151R and P48. These results suggest that the interactions between CD151 and laminin-binding integrins are subject to cell-type-specific regulation.
Sterk
Lotus M T
LM
Division of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.
Geuijen
Cecile A W
CA
van den Berg
José G
JG
Claessen
Nike
N
Weening
Jan J
JJ
Sonnenberg
Arnoud
A
D000911:Antibodies, Monoclonal / Q000276:immunology; D015703:Antigens, CD / Q000276:immunology / Q000378:metabolism*; D000954:Antigens, Surface / Q000378:metabolism*; D002478:Cells, Cultured; D003598:Cytoskeletal Proteins / Q000502:physiology; D049030:Dystroglycans; D000939:Epitopes / Q000276:immunology; D006801:Humans; D039201:Integrin alpha3beta1; D039121:Integrin alpha6beta1; D039161:Integrin alpha6beta4; D016023:Integrins / Q000378:metabolism*; D020014:K562 Cells; D007678:Kidney Glomerulus / Q000378:metabolism / Q000648:ultrastructure; D007684:Kidney Tubules / Q000166:cytology / Q000378:metabolism / Q000648:ultrastructure; D008188:Lutheran Blood-Group System / Q000502:physiology; D008562:Membrane Glycoproteins / Q000502:physiology; D009132:Muscles / Q000033:anatomy & histology / Q000166:cytology / Q000378:metabolism / Q000648:ultrastructure; D017474:Receptors, Laminin / Q000378:metabolism; D012867:Skin / Q000166:cytology / Q000378:metabolism / Q000648:ultrastructure; D060185:Tetraspanin 24
D000911:Antibodies, Monoclonal; D015703:Antigens, CD; D000954:Antigens, Surface; C554715:CD151 protein, human; D003598:Cytoskeletal Proteins; C483081:DAG1 protein, human; D000939:Epitopes; D039201:Integrin alpha3beta1; D039121:Integrin alpha6beta1; D039161:Integrin alpha6beta4; D016023:Integrins; D008188:Lutheran Blood-Group System; D008562:Membrane Glycoproteins; D017474:Receptors, Laminin; D060185:Tetraspanin 24; D049030:Dystroglycans; C082908:integrin alpha7beta1