دورية أكاديمية
أعرض في EDS

Dynamic Scaling Analysis of Molecular Motion within the LAT:Grb2:SOS Protein Network on Membranes.

التفاصيل البيبلوغرافية
العنوان: Dynamic Scaling Analysis of Molecular Motion within the LAT:Grb2:SOS Protein Network on Membranes.
المؤلفون: Huang WYC; Department of Chemistry, University of California, Berkeley, Berkeley, California., Chiang HK; Department of Chemistry, University of California, Berkeley, Berkeley, California., Groves JT; Department of Chemistry, University of California, Berkeley, Berkeley, California. Electronic address: jtgroves@lbl.gov.
المصدر: Biophysical journal [Biophys J] 2017 Oct 17; Vol. 113 (8), pp. 1807-1813.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Cell Press Country of Publication: United States NLM ID: 0370626 Publication Model: Print Cited Medium: Internet ISSN: 1542-0086 (Electronic) Linking ISSN: 00063495 NLM ISO Abbreviation: Biophys J Subsets: MEDLINE
أسماء مطبوعة: Publication: Cambridge, MA : Cell Press
Original Publication: New York, Published by Rockefeller University Press [etc.] for the Biophysical Society.
مواضيع طبية MeSH: Membranes, Artificial*, Adaptor Proteins, Signal Transducing/*metabolism , GRB2 Adaptor Protein/*metabolism , Membrane Proteins/*metabolism , Son of Sevenless Protein, Drosophila/*metabolism, Adaptor Proteins, Signal Transducing/chemistry ; Computer Simulation ; Diffusion ; GRB2 Adaptor Protein/chemistry ; Humans ; Membrane Proteins/chemistry ; Monte Carlo Method ; Motion ; Phosphotyrosine/chemistry ; Polymers/chemistry ; Single Molecule Imaging ; Son of Sevenless Protein, Drosophila/chemistry ; Viscoelastic Substances/chemistry
مستخلص: Biochemical signaling pathways often involve proteins with multiple, modular interaction domains. Signaling activates binding sites, such as by tyrosine phosphorylation, which enables protein recruitment and growth of networked protein assemblies. Although widely observed, the physical properties of the assemblies, as well as the mechanisms by which they function, remain largely unknown. Here we examine molecular mobility within LAT:Grb2:SOS assemblies on supported membranes by single-molecule tracking. Trajectory analysis reveals a discrete temporal transition to subdiffusive motion below a characteristic timescale, indicating that the LAT:Grb2:SOS assembly has the dynamical structure of a loosely entangled polymer. Such dynamical analysis is also applicable in living cells, where it offers another dimension on the characteristics of cellular signaling assemblies.
(Copyright © 2017. Published by Elsevier Inc.)
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معلومات مُعتمدة: U01 CA202241 United States CA NCI NIH HHS
المشرفين على المادة: 0 (Adaptor Proteins, Signal Transducing)
0 (GRB2 Adaptor Protein)
0 (GRB2 protein, human)
0 (LAT protein, human)
0 (Membrane Proteins)
0 (Membranes, Artificial)
0 (Polymers)
0 (Son of Sevenless Protein, Drosophila)
0 (Viscoelastic Substances)
21820-51-9 (Phosphotyrosine)
تواريخ الأحداث: Date Created: 20171019 Date Completed: 20171201 Latest Revision: 20181113
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC5647511
DOI: 10.1016/j.bpj.2017.08.024
PMID: 29045874
قاعدة البيانات: MEDLINE
الوصف
تدمد:1542-0086
DOI:10.1016/j.bpj.2017.08.024