دورية أكاديمية
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Modulation of Functional Phosphorylation Sites by Basic Residues in the Unique Domain of c-Src.

التفاصيل البيبلوغرافية
العنوان: Modulation of Functional Phosphorylation Sites by Basic Residues in the Unique Domain of c-Src.
المؤلفون: Lang A; BioNMR Laboratory, Departament de Química Inorgànica i Orgànica, Universitat de Barcelona (UB), Baldiri Reixac 10-12, 08028 Barcelona, Spain., Fernández A; BioNMR Laboratory, Departament de Química Inorgànica i Orgànica, Universitat de Barcelona (UB), Baldiri Reixac 10-12, 08028 Barcelona, Spain., Diaz-Lobo M; Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST), Baldiri Reixac 10, 08028 Barcelona, Spain., Vilanova M; Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST), Baldiri Reixac 10, 08028 Barcelona, Spain., Cárdenas F; Centres Científics i Tecnològics de la Universitat de Barcelona (CCiTUB), Universitat de Barcelona (UB), Baldiri Reixac 10-12, 08028 Barcelona, Spain., Gairí M; Centres Científics i Tecnològics de la Universitat de Barcelona (CCiTUB), Universitat de Barcelona (UB), Baldiri Reixac 10-12, 08028 Barcelona, Spain., Pons M; BioNMR Laboratory, Departament de Química Inorgànica i Orgànica, Universitat de Barcelona (UB), Baldiri Reixac 10-12, 08028 Barcelona, Spain.
المصدر: Molecules (Basel, Switzerland) [Molecules] 2023 Jun 10; Vol. 28 (12). Date of Electronic Publication: 2023 Jun 10.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: MDPI Country of Publication: Switzerland NLM ID: 100964009 Publication Model: Electronic Cited Medium: Internet ISSN: 1420-3049 (Electronic) Linking ISSN: 14203049 NLM ISO Abbreviation: Molecules Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI, c1995-
مواضيع طبية MeSH: src Homology Domains* , Proto-Oncogene Proteins pp60(c-src)*, Phosphorylation ; Phosphoserine ; Serine
مستخلص: In contrast to the well-studied canonical regulatory mechanisms, the way by which the recently discovered Src N-terminal regulatory element (SNRE) modulates Src activity is not yet well understood. Phosphorylation of serine and threonine residues modulates the charge distribution along the disordered region of the SNRE and may affect a fuzzy complex with the SH3 domain that is believed to act as an information transduction element. The pre-existing positively charged sites can interact with the newly introduced phosphate groups by modulating their acidity, introducing local conformational restrictions, or by coupling various phosphosites into a functional unit. In this paper, we use pH-dependent NMR measurements combined with single point mutations to identify the interactions of basic residues with physiologically important phosphorylated residues and to characterize the effect of these interactions in neighbor residues, thus providing insight into the electrostatic network in the isolated disordered regions and in the entire SNRE. From a methodological point of view, the linear relationships observed between the mutation-induced pKa changes of the phosphate groups of phosphoserine and phosphothreonine and the pH-induced chemical shifts of the NH groups of these residues provide a very convenient alternative to identify interacting phosphate groups without the need to introduce point mutations on specific basic residues.
References: J Mol Biol. 2018 Aug 3;430(16):2342-2359. (PMID: 29626537)
Structure. 2017 Apr 4;25(4):630-640.e4. (PMID: 28319009)
Front Genet. 2014 Jun 30;5:181. (PMID: 25071818)
Mol Cell. 1999 May;3(5):629-38. (PMID: 10360179)
Sci Rep. 2013;3:1295. (PMID: 23416516)
FEBS Lett. 1997 Jul 14;411(2-3):317-21. (PMID: 9271228)
Mol Cancer Res. 2021 Jun;19(6):957-967. (PMID: 33727342)
Am J Cancer Res. 2012;2(4):357-71. (PMID: 22860228)
Nat Rev Cancer. 2004 Jun;4(6):470-80. (PMID: 15170449)
Structure. 1995 Mar 15;3(3):299-307. (PMID: 7540485)
Cell Mol Life Sci. 2011 Oct;68(20):3425-36. (PMID: 21442427)
Structure. 2005 Jun;13(6):861-71. (PMID: 15939018)
J Biomol NMR. 2002 Oct;24(2):149-54. (PMID: 12495031)
Nat Commun. 2022 Jan 25;13(1):472. (PMID: 35078976)
J Biol Chem. 1994 Oct 28;269(43):26885-9. (PMID: 7929427)
Proc Natl Acad Sci U S A. 2022 Aug 2;119(31):e2209201119. (PMID: 35858387)
Biophys J. 2021 Dec 21;120(24):5438-5453. (PMID: 34826385)
Front Mol Biosci. 2018 Apr 30;5:39. (PMID: 29761107)
Oncogene. 2022 Feb;41(7):960-970. (PMID: 34999732)
Breast Cancer Res. 2000;2(3):154-7. (PMID: 11250704)
J Am Chem Soc. 2007 Mar 14;129(10):2971-80. (PMID: 17300195)
J Mol Biol. 2009 Aug 7;391(1):136-48. (PMID: 19520085)
Commun Biol. 2021 Feb 23;4(1):243. (PMID: 33623120)
Structure. 2015 May 5;23(5):893-902. (PMID: 25914053)
Redox Biol. 2021 Apr;40:101842. (PMID: 33388549)
Biomacromolecules. 2023 Feb 13;24(2):714-723. (PMID: 36692364)
Proc Natl Acad Sci U S A. 2013 Aug 13;110(33):13392-7. (PMID: 23901099)
معلومات مُعتمدة: PID2019-104914RB-I00 MICIN (spain); PDC2021-121629-I00 MICIN (Spain); FEDER EQC2019-5587P MICIN/FEDER; ICTS2021-6875 EU Next Generation; ICTS2022-7829 EU Next Generation; IPT17/0019-ISCIII-SGEFI/ERDF Instituto de Salud Carlos III
فهرسة مساهمة: Keywords: ERK2; IDP phosphorylation; SNRE; fuzzy complex; guanidinium–phosphate salt bridge; intrinsically disordered proteins; pKa measurements; phosphoserine; phosphothreonine
المشرفين على المادة: EC 2.7.10.2 (Proto-Oncogene Proteins pp60(c-src))
17885-08-4 (Phosphoserine)
452VLY9402 (Serine)
تواريخ الأحداث: Date Created: 20230628 Date Completed: 20230629 Latest Revision: 20230701
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC10304449
DOI: 10.3390/molecules28124686
PMID: 37375241
قاعدة البيانات: MEDLINE
الوصف
تدمد:1420-3049
DOI:10.3390/molecules28124686