Abstract

Integrins are type I heterodimeric (α/β) cell adhesion molecules. They trigger cell-signaling by recruiting cytosolic molecules to their cytoplasmic tails. Integrin α cytoplasmic tail contributes towards integrin function specificity, an important feature of integrins having different α subunits but sharing the same β subunit. Herein, we show that the src family kinase Hck co-capped selectively with leukocyte integrin α Mβ 2 but not α Lβ 2 or α Xβ 2. This was disrupted when the α M cytoplasmic tail was substituted with that of α L or α X. Co-capping was recovered by α L or α X cytoplasmic tail truncation or forced separation of the α and β cytoplasmic tails via salt-bridge disruption.

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