TY  -  
T1  - Phosphorylation of the α-chain in the integrin LFA-1 enables β2-chain phosphorylation and α-actinin binding required for cell adhesion 
SN  -  /  
UR  - http://hdl.handle.net/10138/303101 
T3  -  
A1  - Jahan, Farhana; Madhavan, Sudarrshan; Rolova, Taisia; Viazmina, Larisa; Grönholm, Mikaela; Gahmberg, Carl G. 
A2  -  
PB  -  
Y1  - 2018 
LA  - eng 
AB  - The integrin leukocyte function-associated antigen-1 (LFA-1) plays a pivotal role in leukocyte adhesion and migration, but the mechanism(s) by which this integrin is regulated has remained incompletely understood. LFA-1 integrin activity requires phosphorylation of its 2-chain and interactions of its cytoplasmic tail with various cellular proteins. The -chain is constitutively phosphorylated and necessary for cellular adhesion, but how the -chain regulates adhesion has remained enigmatic. We now... 
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IS  -  
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KW  - integrin; phosphorylation; leukocyte; adhesion; talin; 14-3-3 protein; filamin; alpha-actinin; FUNCTION-ASSOCIATED ANTIGEN-1; INSIDE-OUT ACTIVATION; CYTOPLASMIC DOMAIN; LEUKOCYTE ADHESION; LIGAND-BINDING; THREONINE PHOSPHORYLATION; T-LYMPHOCYTES; BETA-SUBUNIT; CD18; AFFINITY; 1182 Biochemistry, cell and molecular biology 
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ER  -