Beta2 integrin phosphorylation on Thr758 acts as a molecular switch to regulate 14-3-3 and filamin binding

Leukocyte integrins of the beta2 family are essential for immune cell-cell adhesion. In activated cells, beta2 integrins are phosphorylated on the cytoplasmic Thr758, leading to 14-3-3 protein recruitment to the beta2 integrin. The mutation of this phosphorylation site impairs cell adhesion, actin r...

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Bibliographic Details
Published in:Blood 2008-09, Vol.112 (5), p.1853
Main Authors: Takala, Heikki, Nurminen, Elisa, Nurmi, Susanna M, Aatonen, Maria, Strandin, Tomas, Takatalo, Maarit, Kiema, Tiila, Gahmberg, Carl G, Ylänne, Jari, Fagerholm, Susanna C
Format: Article
Language:English
Subjects:
14-3-3 Proteins - chemistry
14-3-3 Proteins - metabolism
Amino Acid Substitution
Binding Sites
CD18 Antigens - chemistry
CD18 Antigens - genetics
CD18 Antigens - metabolism
Cell Adhesion
Contractile Proteins - chemistry
Contractile Proteins - metabolism
Filamins
Humans
In Vitro Techniques
Intercellular Adhesion Molecule-1 - metabolism
Jurkat Cells
Microfilament Proteins - chemistry
Microfilament Proteins - metabolism
Models, Molecular
Multiprotein Complexes
Phosphorylation
Protein Binding
Protein Interaction Domains and Motifs
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Static Electricity
T-Lymphocytes - metabolism
Talin - metabolism
Threonine - chemistry
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