2brq: Difference between revisions

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==Overview==

The ability of adhesion receptors to transmit biochemical signals and, mechanical force across cell membranes depends on interactions with the, actin cytoskeleton. Filamins are large, actin-crosslinking proteins that, connect multiple transmembrane and signaling proteins to the cytoskeleton., Here, we describe the high-resolution structure of an interface between, filamin A and an integrin adhesion receptor. When bound, the integrin beta, cytoplasmic tail forms an extended beta strand that interacts with beta, strands C and D of the filamin immunoglobulin-like domain (IgFLN) 21. This, interface is common to many integrins, and we suggest it is a prototype, for other IgFLN domain interactions. Notably, the structurally defined, filamin binding site overlaps with that of the integrin-regulator talin, and these proteins compete for binding to integrin tails, allowing, integrin-filamin interactions to impact talin-dependent integrin, activation. Phosphothreonine-mimicking mutations inhibit filamin, but not, talin, binding, indicating that kinases may modulate this competition and, provide additional means to control integrin functions.

The ability of adhesion receptors to transmit biochemical signals and mechanical force across cell membranes depends on interactions with the actin cytoskeleton. Filamins are large, actin-crosslinking proteins that connect multiple transmembrane and signaling proteins to the cytoskeleton. Here, we describe the high-resolution structure of an interface between filamin A and an integrin adhesion receptor. When bound, the integrin beta cytoplasmic tail forms an extended beta strand that interacts with beta strands C and D of the filamin immunoglobulin-like domain (IgFLN) 21. This interface is common to many integrins, and we suggest it is a prototype for other IgFLN domain interactions. Notably, the structurally defined filamin binding site overlaps with that of the integrin-regulator talin, and these proteins compete for binding to integrin tails, allowing integrin-filamin interactions to impact talin-dependent integrin activation. Phosphothreonine-mimicking mutations inhibit filamin, but not talin, binding, indicating that kinases may modulate this competition and provide additional means to control integrin functions.

==Disease==

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[[Category: Homo sapiens]]

[[Category: Protein complex]]

[[Category: Kiema, T.R.]]

[[Category: Kiema, T R.]]

[[Category: Ylanne, J.]]

[[Category: GOL]]

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[[Category: receptor]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:56 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The ability of adhesion receptors to transmit biochemical signals and, mechanical force across cell membranes depends on interactions with the, actin cytoskeleton. Filamins are large, actin-crosslinking proteins that, connect multiple transmembrane and signaling proteins to the cytoskeleton., Here, we describe the high-resolution structure of an interface between, filamin A and an integrin adhesion receptor. When bound, the integrin beta, cytoplasmic tail forms an extended beta strand that interacts with beta, strands C and D of the filamin immunoglobulin-like domain (IgFLN) 21. This, interface is common to many integrins, and we suggest it is a prototype, for other IgFLN domain interactions. Notably, the structurally defined, filamin binding site overlaps with that of the integrin-regulator talin, and these proteins compete for binding to integrin tails, allowing, integrin-filamin interactions to impact talin-dependent integrin, activation. Phosphothreonine-mimicking mutations inhibit filamin, but not, talin, binding, indicating that kinases may modulate this competition and, provide additional means to control integrin functions.
+The ability of adhesion receptors to transmit biochemical signals and mechanical force across cell membranes depends on interactions with the actin cytoskeleton. Filamins are large, actin-crosslinking proteins that connect multiple transmembrane and signaling proteins to the cytoskeleton. Here, we describe the high-resolution structure of an interface between filamin A and an integrin adhesion receptor. When bound, the integrin beta cytoplasmic tail forms an extended beta strand that interacts with beta strands C and D of the filamin immunoglobulin-like domain (IgFLN) 21. This interface is common to many integrins, and we suggest it is a prototype for other IgFLN domain interactions. Notably, the structurally defined filamin binding site overlaps with that of the integrin-regulator talin, and these proteins compete for binding to integrin tails, allowing integrin-filamin interactions to impact talin-dependent integrin activation. Phosphothreonine-mimicking mutations inhibit filamin, but not talin, binding, indicating that kinases may modulate this competition and provide additional means to control integrin functions.
 ==Disease==
@@ Line 16: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Protein complex]]
-[[Category: Kiema, T.R.]]
+[[Category: Kiema, T R.]]
 [[Category: Ylanne, J.]]
 [[Category: GOL]]
@@ Line 31: / Line 31: @@
 [[Category: receptor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:27:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:56 2008''