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Diversity of Structural, Dynamic, and Environmental Effects Explain a Distinctive Functional Role of Transmembrane Domains in the Insulin Receptor Subfamily.

التفاصيل البيبلوغرافية
العنوان: Diversity of Structural, Dynamic, and Environmental Effects Explain a Distinctive Functional Role of Transmembrane Domains in the Insulin Receptor Subfamily.
المؤلفون: Bershatsky YV; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia., Kuznetsov AS; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia., Idiatullina AR; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia., Bocharova OV; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia., Dolotova SM; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia., Gavrilenkova AA; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia., Serova OV; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia., Deyev IE; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia., Rakitina TV; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia., Zangieva OT; Federal State Budgetary Institution 'National Medical and Surgical Center named after N.I. Pirogov', Moscow 105203, Russia., Pavlov KV; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.; Federal Clinical Center of Physical-Chemical Medicine of FMBA, Moscow 119435, Russia., Batishchev OV; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia.; Frumkin Institute of Physical Chemistry and Electrochemistry of Russian Academy of Sciences, Moscow 119071, Russia., Britikov VV; Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, 220141 Minsk, Belarus., Usanov SA; Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, 220141 Minsk, Belarus., Arseniev AS; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia., Efremov RG; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia.; Department of Applied Mathematics, National Research University Higher School of Economics, Moscow 101000, Russia., Bocharov EV; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia.
المصدر: International journal of molecular sciences [Int J Mol Sci] 2023 Feb 15; Vol. 24 (4). Date of Electronic Publication: 2023 Feb 15.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: MDPI Country of Publication: Switzerland NLM ID: 101092791 Publication Model: Electronic Cited Medium: Internet ISSN: 1422-0067 (Electronic) Linking ISSN: 14220067 NLM ISO Abbreviation: Int J Mol Sci Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI, [2000-
مواضيع طبية MeSH: Receptor, Insulin*/chemistry , Receptor, Insulin*/physiology , Drug Development*, Humans ; Protein Domains ; Signal Transduction
مستخلص: Human InsR, IGF1R, and IRR receptor tyrosine kinases (RTK) of the insulin receptor subfamily play an important role in signaling pathways for a wide range of physiological processes and are directly associated with many pathologies, including neurodegenerative diseases. The disulfide-linked dimeric structure of these receptors is unique among RTKs. Sharing high sequence and structure homology, the receptors differ dramatically in their localization, expression, and functions. In this work, using high-resolution NMR spectroscopy supported by atomistic computer modeling, conformational variability of the transmembrane domains and their interactions with surrounding lipids were found to differ significantly between representatives of the subfamily. Therefore, we suggest that the heterogeneous and highly dynamic membrane environment should be taken into account in the observed diversity of the structural/dynamic organization and mechanisms of activation of InsR, IGF1R, and IRR receptors. This membrane-mediated control of receptor signaling offers an attractive prospect for the development of new targeted therapies for diseases associated with dysfunction of insulin subfamily receptors.
References: Nature. 2001 Dec 13;414(6865):799-806. (PMID: 11742412)
J Biol Chem. 1995 Aug 11;270(32):19041-5. (PMID: 7642566)
Cell. 2010 Jun 25;141(7):1117-34. (PMID: 20602996)
Aging Cell. 2019 Jun;18(3):e12932. (PMID: 30884121)
J Biol Chem. 2019 Nov 22;294(47):17790-17798. (PMID: 31615897)
Cell Metab. 2011 Jun 8;13(6):679-89. (PMID: 21641549)
Biochim Biophys Acta Biomembr. 2020 Nov 1;1862(11):183417. (PMID: 32710851)
Front Endocrinol (Lausanne). 2016 Jun 20;7:68. (PMID: 27379020)
Nature. 2018 Apr 5;556(7699):122-125. (PMID: 29512653)
J Biomol NMR. 2013 Jul;56(3):227-41. (PMID: 23728592)
Biochemistry. 2017 Mar 28;56(12):1697-1705. (PMID: 28291355)
J Pharmacol Sci. 2019 Jul;140(3):300-304. (PMID: 31353211)
Nat Commun. 2019 Oct 8;10(1):4567. (PMID: 31594955)
FEBS J. 2016 Dec;283(24):4424-4451. (PMID: 27350538)
J Am Chem Soc. 2013 Jun 5;135(22):8105-8. (PMID: 23679838)
Prog Nucl Magn Reson Spectrosc. 2009 Apr 5;54(3-4):141-165. (PMID: 20160946)
Curr Opin Struct Biol. 2016 Aug;39:115-123. (PMID: 27423296)
Biochim Biophys Acta Gen Subj. 2019 Jan;1863(1):82-95. (PMID: 30253204)
Nat Rev Neurol. 2012 Jun 19;8(7):360-2. (PMID: 22710630)
J Biomol NMR. 2006 Oct;36(2):123-36. (PMID: 17013683)
J Mol Biol. 2022 Mar 15;434(5):167458. (PMID: 35074483)
Nature. 2006 Sep 14;443(7108):218-21. (PMID: 16957736)
Arch Physiol Biochem. 2008 Feb;114(1):23-37. (PMID: 18465356)
Elife. 2019 Aug 22;8:. (PMID: 31436533)
Structure. 2016 Mar 1;24(3):469-76. (PMID: 26853939)
Elife. 2014 Sep 25;3:. (PMID: 25255214)
J Biol Chem. 1983 Aug 25;258(16):10020-6. (PMID: 6411700)
Biochim Biophys Acta Biomembr. 2019 Apr 1;1861(4):819-826. (PMID: 30682326)
Biochim Biophys Acta. 2014 May;1838(5):1313-21. (PMID: 24440425)
Methods Mol Biol. 2004;278:353-78. (PMID: 15318003)
J Biomol Struct Dyn. 1993 Dec;11(3):483-507. (PMID: 8129869)
FASEB J. 1999 Aug;13(11):1347-57. (PMID: 10428759)
J Mol Endocrinol. 2011 Jun 17;47(1):R1-10. (PMID: 21498522)
Endocrinology. 1995 Feb;136(2):558-61. (PMID: 7835288)
J Biol Chem. 1992 Jun 25;267(18):12416-9. (PMID: 1618747)
J Biomol NMR. 2011 Jan;49(1):9-15. (PMID: 21190063)
J Cell Biol. 2018 May 7;217(5):1643-1649. (PMID: 29453311)
EMBO J. 1986 Oct;5(10):2503-12. (PMID: 2877871)
J Magn Reson. 2012 Oct;223:1-10. (PMID: 22960668)
Biochim Biophys Acta Biomembr. 2017 Sep;1859(9 Pt A):1417-1429. (PMID: 28131853)
Biochim Biophys Acta Biomembr. 2017 Apr;1859(4):561-576. (PMID: 27884807)
Curr Protein Pept Sci. 2011 Dec;12(8):760-6. (PMID: 22044142)
Nature. 1985 Feb 28-Mar 6;313(6005):756-61. (PMID: 2983222)
J Biol Chem. 2021 Jan-Jun;296:100534. (PMID: 33713705)
Cell. 1985 Apr;40(4):747-58. (PMID: 2859121)
Cell. 2013 Jan 31;152(3):557-69. (PMID: 23374350)
J Biomol NMR. 1998 Feb;11(2):221-6. (PMID: 9679296)
Anal Biochem. 1987 Nov 1;166(2):368-79. (PMID: 2449095)
Protein Expr Purif. 2016 Jul;123:105-11. (PMID: 27071311)
Nat Commun. 2018 Feb 26;9(1):821. (PMID: 29483580)
Bioinformatics. 2014 Mar 15;30(6):889-90. (PMID: 24202542)
معلومات مُعتمدة: 23-44-10021 Russian Science Foundation; Х23РНФ-091 Belarusian Republican Foundation for Basic Research
فهرسة مساهمة: Keywords: NMR; insulin receptor subfamily; molecular dynamics; protein-lipid interactions; receptor tyrosine kinases; structural-dynamical properties; transmembrane domain
المشرفين على المادة: EC 2.7.10.1 (Receptor, Insulin)
تواريخ الأحداث: Date Created: 20230225 Date Completed: 20230329 Latest Revision: 20230329
رمز التحديث: 20230331
مُعرف محوري في PubMed: PMC9965288
DOI: 10.3390/ijms24043906
PMID: 36835322
قاعدة البيانات: MEDLINE
الوصف
تدمد:1422-0067
DOI:10.3390/ijms24043906