Publication Date:
2003-10-04
Description:
Control of integrin affinity for ligands (integrin activation) is essential for normal cell adhesion, migration, and assembly of an extracellular matrix. Integrin activation is usually mediated through the integrin beta subunit cytoplasmic tail and can be regulated by many different biochemical signaling pathways. We report that specific binding of the cytoskeletal protein talin to integrin beta subunit cytoplasmic tails leads to the conformational rearrangements of integrin extracellular domains that increase their affinity. Thus, regulated binding of talin to integrin beta tails is a final common element of cellular signaling cascades that control integrin activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tadokoro, Seiji -- Shattil, Sanford J -- Eto, Koji -- Tai, Vera -- Liddington, Robert C -- de Pereda, Jose M -- Ginsberg, Mark H -- Calderwood, David A -- New York, N.Y. -- Science. 2003 Oct 3;302(5642):103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, The Scripps Research Institute, The Burnham Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14526080" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Amino Acid Substitution
;
Animals
;
Antibodies, Monoclonal/immunology
;
Antigens, CD29/chemistry/metabolism
;
Cell Line
;
Fibronectins/metabolism
;
Humans
;
Integrin beta Chains/chemistry/*metabolism
;
Integrin beta3/chemistry/metabolism
;
Molecular Sequence Data
;
Mutation
;
Platelet Glycoprotein GPIIb-IIIa Complex/chemistry/immunology/metabolism
;
Protein Binding
;
Protein Conformation
;
Protein Structure, Tertiary
;
RNA, Small Interfering
;
Recombinant Proteins/metabolism
;
*Signal Transduction
;
Talin/*metabolism
;
Transfection
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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