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Phosphorylation of Doc2 by EphB2 modulates Munc13-mediated SNARE complex assembly and neurotransmitter release.

التفاصيل البيبلوغرافية
العنوان: Phosphorylation of Doc2 by EphB2 modulates Munc13-mediated SNARE complex assembly and neurotransmitter release.
المؤلفون: Zhang H; Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, 430074 Wuhan, China., Lei M; Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, 430074 Wuhan, China., Zhang Y; Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, 430074 Wuhan, China., Li H; Institute for Brain Research, Wuhan Center of Brain Science, Huazhong University of Science and Technology, Wuhan 430030, China.; Department of Pathophysiology, School of Basic Medicine and Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China., He Z; Department of Pathogen Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, 430030 Wuhan, China., Xie S; Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, 430074 Wuhan, China., Zhu L; Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, 430074 Wuhan, China., Wang S; Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, 430074 Wuhan, China., Liu J; Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, 430074 Wuhan, China., Li Y; Department of Pathogen Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, 430030 Wuhan, China., Lu Y; Institute for Brain Research, Wuhan Center of Brain Science, Huazhong University of Science and Technology, Wuhan 430030, China.; Department of Pathophysiology, School of Basic Medicine and Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China., Ma C; Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, 430074 Wuhan, China.; Institute for Brain Research, Wuhan Center of Brain Science, Huazhong University of Science and Technology, Wuhan 430030, China.
المصدر: Science advances [Sci Adv] 2024 May 17; Vol. 10 (20), pp. eadi7024. Date of Electronic Publication: 2024 May 17.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: American Association for the Advancement of Science Country of Publication: United States NLM ID: 101653440 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2375-2548 (Electronic) Linking ISSN: 23752548 NLM ISO Abbreviation: Sci Adv Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, DC : American Association for the Advancement of Science, [2015]-
مواضيع طبية MeSH: SNARE Proteins*/metabolism , Neurotransmitter Agents*/metabolism , Nerve Tissue Proteins*/metabolism , Receptor, EphB2*/metabolism , Receptor, EphB2*/genetics , Calcium-Binding Proteins*/metabolism , Synaptic Transmission*, Animals ; Phosphorylation ; Protein Binding ; Humans ; Mice ; Rats
مستخلص: At the synapse, presynaptic neurotransmitter release is tightly controlled by release machinery, involving the soluble N -ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins and Munc13. The Ca 2+ sensor Doc2 cooperates with Munc13 to regulate neurotransmitter release, but the underlying mechanisms remain unclear. In our study, we have characterized the binding mode between Doc2 and Munc13 and found that Doc2 originally occludes Munc13 to inhibit SNARE complex assembly. Moreover, our investigation unveiled that EphB2, a presynaptic adhesion molecule (SAM) with inherent tyrosine kinase functionality, exhibits the capacity to phosphorylate Doc2. This phosphorylation attenuates Doc2 block on Munc13 to promote SNARE complex assembly, which functionally induces spontaneous release and synaptic augmentation. Consistently, application of a Doc2 peptide that interrupts Doc2-Munc13 interplay impairs excitatory synaptic transmission and leads to dysfunction in spatial learning and memory. These data provide evidence that SAMs modulate neurotransmitter release by controlling SNARE complex assembly.
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تواريخ الأحداث: Date Created: 20240517 Date Completed: 20240517 Latest Revision: 20240617
رمز التحديث: 20240618
مُعرف محوري في PubMed: PMC11100570
DOI: 10.1126/sciadv.adi7024
PMID: 38758791
قاعدة البيانات: MEDLINE
الوصف
تدمد:2375-2548
DOI:10.1126/sciadv.adi7024