TY - JOUR
T1 - P marks the spot
T2 - site-specific integrin phosphorylation regulates molecular interactions
AU - Fagerholm, Susanna C.
AU - Hilden, Tiina J.
AU - Gahmberg, Carl G.
PY - 2004/9
Y1 - 2004/9
N2 - Integrins are heterodimeric adhesion receptors at the cell membrane that function as two-way signaling devices. The short intracellular tails of integrins are devoid of catalytic activity, but are nevertheless important for adhesion and signaling, presumably, through interactions with cytoplasmic molecules. Recently, the structure of the intracellular tails has been investigated using NMR, giving important new insight into how integrins might be regulated, but many questions remain unanswered. Signaling by many cell-surface receptors involves protein phosphorylation; over the past few years, phosphorylation of the integrin tails at specific sites has started to emerge as a dynamic mechanism that regulates molecular interactions between integrins and cytoplasmic molecules. This phosphorylation might give rise to signaling specificity and fine-tuning of the integrin-mediated responses.
AB - Integrins are heterodimeric adhesion receptors at the cell membrane that function as two-way signaling devices. The short intracellular tails of integrins are devoid of catalytic activity, but are nevertheless important for adhesion and signaling, presumably, through interactions with cytoplasmic molecules. Recently, the structure of the intracellular tails has been investigated using NMR, giving important new insight into how integrins might be regulated, but many questions remain unanswered. Signaling by many cell-surface receptors involves protein phosphorylation; over the past few years, phosphorylation of the integrin tails at specific sites has started to emerge as a dynamic mechanism that regulates molecular interactions between integrins and cytoplasmic molecules. This phosphorylation might give rise to signaling specificity and fine-tuning of the integrin-mediated responses.
U2 - 10.1016/j.tibs.2004.07.005
DO - 10.1016/j.tibs.2004.07.005
M3 - Article
C2 - 15337124
SN - 0968-0004
VL - 29
SP - 504
EP - 512
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
IS - 9
ER -