دورية أكاديمية
Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations.
| العنوان: | Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations. |
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| المؤلفون: | Li R; Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA., Mitra N, Gratkowski H, Vilaire G, Litvinov R, Nagasami C, Weisel JW, Lear JD, DeGrado WF, Bennett JS |
| المصدر: | Science (New York, N.Y.) [Science] 2003 May 02; Vol. 300 (5620), pp. 795-8. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Association for the Advancement of Science Country of Publication: United States NLM ID: 0404511 Publication Model: Print Cited Medium: Internet ISSN: 1095-9203 (Electronic) Linking ISSN: 00368075 NLM ISO Abbreviation: Science Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Original Publication: New York, N.Y. : [s.n.] 1880- |
| مواضيع طبية MeSH: | Protein Structure, Secondary*, Cell Membrane/*chemistry , Platelet Glycoprotein GPIIb-IIIa Complex/*chemistry , Platelet Glycoprotein GPIIb-IIIa Complex/*metabolism, Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Antibodies, Monoclonal/metabolism ; Biopolymers ; CHO Cells ; Cell Adhesion ; Cricetinae ; Cricetulus ; Dimerization ; Fibrinogen/metabolism ; Fluorescein-5-isothiocyanate ; Focal Adhesion Protein-Tyrosine Kinases ; Ligands ; Microscopy, Fluorescence ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Platelet Glycoprotein GPIIb-IIIa Complex/genetics ; Protein Conformation ; Protein Structure, Tertiary ; Protein-Tyrosine Kinases/metabolism ; Receptor Aggregation |
| مستخلص: | Transmembrane helices of integrin alpha and beta subunits have been implicated in the regulation of integrin activity. Two mutations, glycine-708 to asparagine-708 (G708N)and methionine-701 to asparagine-701, in the transmembrane helix of the beta3 subunit enabled integrin alphaIIbbeta3 to constitutively bind soluble fibrinogen. Further characterization of the G708N mutant revealed that it induced alphaIIbbeta3 clustering and constitutive phosphorylation of focal adhesion kinase. This mutation also enhanced the tendency of the transmembrane helix to form homotrimers. These results suggest that homomeric associations involving transmembrane domains provide a driving force for integrin activation. They also suggest a structural basis for the coincidence of integrin activation and clustering. |
| التعليقات: | Comment in: Science. 2003 May 2;300(5620):755-6. (PMID: 12730590) |
| معلومات مُعتمدة: | K01 CA096706 United States CA NCI NIH HHS; HL40387 United States HL NHLBI NIH HHS; HL54500 United States HL NHLBI NIH HHS |
| المشرفين على المادة: | 0 (Antibodies, Monoclonal) 0 (Biopolymers) 0 (Ligands) 0 (Platelet Glycoprotein GPIIb-IIIa Complex) 9001-32-5 (Fibrinogen) EC 2.7.10.1 (Protein-Tyrosine Kinases) EC 2.7.10.2 (Focal Adhesion Protein-Tyrosine Kinases) I223NX31W9 (Fluorescein-5-isothiocyanate) |
| تواريخ الأحداث: | Date Created: 20030506 Date Completed: 20030527 Latest Revision: 20161019 |
| رمز التحديث: | 20240627 |
| DOI: | 10.1126/science.1079441 |
| PMID: | 12730600 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1095-9203 |
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| DOI: | 10.1126/science.1079441 |