دورية أكاديمية
أعرض في EDS

Transmembrane helix interactions regulate oligomerization of the receptor tyrosine kinase EphA2.

التفاصيل البيبلوغرافية
العنوان: Transmembrane helix interactions regulate oligomerization of the receptor tyrosine kinase EphA2.
المؤلفون: Wirth D; Department of Materials Science and Engineering, Johns Hopkins University, Baltimore, Maryland, USA., Özdemir E; Department of Materials Science and Engineering, Johns Hopkins University, Baltimore, Maryland, USA., Wimley WC; Department of Biochemistry and Molecular Biology, Tulane University School of Medicine, New Orleans, Louisiana, USA., Pasquale EB; Cancer Metabolism and Microenvironment Program, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, California, USA., Hristova K; Department of Materials Science and Engineering, Johns Hopkins University, Baltimore, Maryland, USA. Electronic address: kh@jhu.edu.
المصدر: The Journal of biological chemistry [J Biol Chem] 2024 Jul; Vol. 300 (7), pp. 107441. Date of Electronic Publication: 2024 Jun 03.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
أسماء مطبوعة: Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
مواضيع طبية MeSH: Receptor, EphA2*/metabolism , Receptor, EphA2*/chemistry , Receptor, EphA2*/genetics , Protein Multimerization*, Humans ; Fluorescence Resonance Energy Transfer ; Cell Membrane/metabolism ; Protein Conformation, alpha-Helical ; Mutation
مستخلص: The transmembrane helices of receptor tyrosine kinases (RTKs) have been proposed to switch between two different dimeric conformations, one associated with the inactive RTK and the other with the active RTK. Furthermore, recent work has demonstrated that some full-length RTKs are associated into oligomers that are larger than dimers, raising questions about the roles of the TM helices in the assembly and function of these oligomers. Here we probe the roles of the TM helices in the assembly of EphA2 RTK oligomers in the plasma membrane. We employ mutagenesis to evaluate the relevance of a published NMR dimeric structure of the isolated EphA2 TM helix in the context of the full-length EphA2 in the plasma membrane. We use two fluorescence methods, Förster Resonance Energy Transfer and Fluorescence Intensity Fluctuations spectrometry, which yield complementary information about the EphA2 oligomerization process. These studies reveal that the TM helix mutations affect the stability, structure, and size of EphA2 oligomers. However, the effects are multifaceted and point to a more complex role of the TM helix than the one expected from the "TM dimer switch" model.
Competing Interests: Conflict of interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)
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فهرسة مساهمة: Keywords: EphA2; oligomerization; receptor tyrosine kinase; single-pass membrane receptor; transmembrane domain
المشرفين على المادة: EC 2.7.10.1 (Receptor, EphA2)
0 (EPHA2 protein, human)
تواريخ الأحداث: Date Created: 20240605 Date Completed: 20240725 Latest Revision: 20240725
رمز التحديث: 20240726
مُعرف محوري في PubMed: PMC11263659
DOI: 10.1016/j.jbc.2024.107441
PMID: 38838777
قاعدة البيانات: MEDLINE
الوصف
تدمد:1083-351X
DOI:10.1016/j.jbc.2024.107441