دورية أكاديمية
أعرض في EDS

Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A.

التفاصيل البيبلوغرافية
العنوان: Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A.
المؤلفون: Olivieri C; Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, United States., Wang Y; Department of Chemistry and Supercomputing Institute, University of Minnesota, Minneapolis, United States.; Shenzhen Bay Laboratory, Shenzhen, China., Li GC; Department of Chemistry and Supercomputing Institute, University of Minnesota, Minneapolis, United States., V S M; Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, United States., Kim J; Department of Chemistry and Supercomputing Institute, University of Minnesota, Minneapolis, United States., Stultz BR; Department of Chemistry, Bethel University, Saint Paul, United States., Neibergall M; Department of Chemistry, Bethel University, Saint Paul, United States., Porcelli F; DIBAF, University of Tuscia, Largo dell' Università, Viterbo, Italy., Muretta JM; Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, United States., Thomas DD; Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, United States., Gao J; Department of Chemistry and Supercomputing Institute, University of Minnesota, Minneapolis, United States.; Laboratory of Computational Chemistry and Drug Design, Peking University Shenzhen Graduate School, Shenzhen, China., Blumenthal DK; Department of Pharmacology and Toxicology, University of Utah, Salt Lake City, United States., Taylor SS; Department of Chemistry and Biochemistry and Pharmacology, University of California, San Diego, La Jolla, United States., Veglia G; Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, United States.; Department of Chemistry and Supercomputing Institute, University of Minnesota, Minneapolis, United States.
المصدر: ELife [Elife] 2020 Apr 27; Vol. 9. Date of Electronic Publication: 2020 Apr 27.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
اللغة: English
بيانات الدورية: Publisher: eLife Sciences Publications, Ltd Country of Publication: England NLM ID: 101579614 Publication Model: Electronic Cited Medium: Internet ISSN: 2050-084X (Electronic) Linking ISSN: 2050084X NLM ISO Abbreviation: Elife Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Cambridge, UK : eLife Sciences Publications, Ltd., 2012-
مواضيع طبية MeSH: Cyclic AMP-Dependent Protein Kinases/*metabolism , Intracellular Signaling Peptides and Proteins/*metabolism , Protein Kinase Inhibitors/*metabolism, Active Transport, Cell Nucleus ; Animals ; Cyclic AMP-Dependent Protein Kinases/genetics ; Cytoplasm ; Escherichia coli ; Intracellular Signaling Peptides and Proteins/genetics ; Karyopherins/genetics ; Karyopherins/metabolism ; Magnetic Resonance Spectroscopy ; Markov Chains ; Mice ; Rabbits ; Receptors, Cytoplasmic and Nuclear/genetics ; Receptors, Cytoplasmic and Nuclear/metabolism ; Exportin 1 Protein
مستخلص: In the nucleus, the spatiotemporal regulation of the catalytic subunit of cAMP-dependent protein kinase A (PKA-C) is orchestrated by an intrinsically disordered protein kinase inhibitor, PKI, which recruits the CRM1/RanGTP nuclear exporting complex. How the PKA-C/PKI complex assembles and recognizes CRM1/RanGTP is not well understood. Using NMR, SAXS, fluorescence, metadynamics, and Markov model analysis, we determined the multi-state recognition pathway for PKI. After a fast binding step in which PKA-C selects PKI's most competent conformations, PKI folds upon binding through a slow conformational rearrangement within the enzyme's binding pocket. The high-affinity and pseudo-substrate regions of PKI become more structured and the transient interactions with the kinase augment the helical content of the nuclear export sequence, which is then poised to recruit the CRM1/RanGTP complex for nuclear translocation. The multistate binding mechanism featured by PKA-C/PKI complex represents a paradigm on how disordered, ancillary proteins (or protein domains) are able to operate multiple functions such as inhibiting the kinase while recruiting other regulatory proteins for nuclear export.
Competing Interests: CO, YW, GL, MV, JK, BS, MN, FP, JM, DT, JG, DB, ST, GV No competing interests declared
(© 2020, Olivieri et al.)
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معلومات مُعتمدة: R01 GM046736 United States GM NIGMS NIH HHS; R01 AR032961 United States AR NIAMS NIH HHS; GM 46736 United States GM NIGMS NIH HHS; R01 GM100310 United States GM NIGMS NIH HHS; R01 HL139065 United States HL NHLBI NIH HHS; R35 GM130389 United States GM NIGMS NIH HHS
فهرسة مساهمة: Keywords: E. coli; isotopic labeling; molecular biophysics; protein expression; recombinant dna; structural biology
المشرفين على المادة: 0 (Intracellular Signaling Peptides and Proteins)
0 (Karyopherins)
0 (Protein Kinase Inhibitors)
0 (Receptors, Cytoplasmic and Nuclear)
EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases)
تواريخ الأحداث: Date Created: 20200428 Date Completed: 20210324 Latest Revision: 20240214
رمز التحديث: 20240214
مُعرف محوري في PubMed: PMC7234811
DOI: 10.7554/eLife.55607
PMID: 32338601
قاعدة البيانات: MEDLINE
الوصف
تدمد:2050-084X
DOI:10.7554/eLife.55607