دورية أكاديمية
أعرض في EDS

Ubiquitin ligase and signalling hub MYCBP2 is required for efficient EPHB2 tyrosine kinase receptor function.

التفاصيل البيبلوغرافية
العنوان: Ubiquitin ligase and signalling hub MYCBP2 is required for efficient EPHB2 tyrosine kinase receptor function.
المؤلفون: Chang C; Institut de recherches cliniques de Montréal (IRCM), Montréal, Canada.; Integrated Program in Neuroscience, McGill University, Montréal, Canada., Banerjee SL; Institut de recherches cliniques de Montréal (IRCM), Montréal, Canada.; Division of Experimental Medicine, McGill University, Montréal, Canada., Park SS; Institut de recherches cliniques de Montréal (IRCM), Montréal, Canada.; Integrated Program in Neuroscience, McGill University, Montréal, Canada., Zhang XL; Institut de recherches cliniques de Montréal (IRCM), Montréal, Canada., Cotnoir-White D; Institut de recherches cliniques de Montréal (IRCM), Montréal, Canada., Opperman KJ; Center for Integrative Brain Research, Seattle Children's Research Institute, Seattle, United States., Desbois M; Center for Integrative Brain Research, Seattle Children's Research Institute, Seattle, United States.; School of Life Sciences, Keele University, Keele, United Kingdom., Grill B; Center for Integrative Brain Research, Seattle Children's Research Institute, Seattle, United States.; Department of Pediatrics, University of Washington School of Medicine, Seattle, United States.; Department of Pharmacology, University of Washington School of Medicine, Seattle, United States., Kania A; Institut de recherches cliniques de Montréal (IRCM), Montréal, Canada.; Integrated Program in Neuroscience, McGill University, Montréal, Canada.; Division of Experimental Medicine, McGill University, Montréal, Canada.; Department of Anatomy and Cell Biology, McGill University, Montréal, Canada.
المصدر: ELife [Elife] 2024 Jan 30; Vol. 12. Date of Electronic Publication: 2024 Jan 30.
نوع المنشور: Journal Article
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: Adaptor Proteins, Signal Transducing*/genetics , F-Box Proteins* , Receptor, EphB2*/genetics , Ubiquitin-Protein Ligases*/genetics, Animals ; Humans ; Caenorhabditis elegans/genetics ; Signal Transduction ; Ubiquitin ; Ubiquitination
مستخلص: Eph receptor tyrosine kinases participate in a variety of normal and pathogenic processes during development and throughout adulthood. This versatility is likely facilitated by the ability of Eph receptors to signal through diverse cellular signalling pathways: primarily by controlling cytoskeletal dynamics, but also by regulating cellular growth, proliferation, and survival. Despite many proteins linked to these signalling pathways interacting with Eph receptors, the specific mechanisms behind such links and their coordination remain to be elucidated. In a proteomics screen for novel EPHB2 multi-effector proteins, we identified human MYC binding protein 2 (MYCBP2 or PAM or Phr1). MYCBP2 is a large signalling hub involved in diverse processes such as neuronal connectivity, synaptic growth, cell division, neuronal survival, and protein ubiquitination. Our biochemical experiments demonstrate that the formation of a complex containing EPHB2 and MYCBP2 is facilitated by FBXO45, a protein known to select substrates for MYCBP2 ubiquitin ligase activity. Formation of the MYCBP2-EPHB2 complex does not require EPHB2 tyrosine kinase activity and is destabilised by binding of ephrin-B ligands, suggesting that the MYCBP2-EPHB2 association is a prelude to EPHB2 signalling. Paradoxically, the loss of MYCBP2 results in increased ubiquitination of EPHB2 and a decrease of its protein levels suggesting that MYCBP2 stabilises EPHB2. Commensurate with this effect, our cellular experiments reveal that MYCBP2 is essential for efficient EPHB2 signalling responses in cell lines and primary neurons. Finally, our genetic studies in Caenorhabditis elegans provide in vivo evidence that the ephrin receptor VAB-1 displays genetic interactions with known MYCBP2 binding proteins. Together, our results align with the similarity of neurodevelopmental phenotypes caused by MYCBP2 and EPHB2 loss of function, and couple EPHB2 to a signalling effector that controls diverse cellular functions.
Competing Interests: CC, SB, SP, XZ, DC, KO, MD, BG, AK No competing interests declared
(© 2023, Chang et al.)
التعليقات: Update of: bioRxiv. 2023 Oct 28;:. (PMID: 37693478)
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معلومات مُعتمدة: PJT-153053 Canada CAPMC CIHR; PJT-162225 Canada CAPMC CIHR; R01 NS072129 United States NH NIH HHS; MOP-77556 Canada CAPMC CIHR; PJT-159839 Canada CAPMC CIHR; R01 NS072129 United States NS NINDS NIH HHS
فهرسة مساهمة: Keywords: C. elegans; Eph receptor; Mycbp2; cell biology; chicken; developmental biology; human; mouse; neuron; proteomics; rat; signalling hub
المشرفين على المادة: 0 (Adaptor Proteins, Signal Transducing)
0 (F-Box Proteins)
0 (FBXO45 protein, human)
EC 2.3.2.27 (MYCBP2 protein, human)
EC 2.7.10.1 (Receptor, EphB2)
0 (Ubiquitin)
EC 2.3.2.27 (Ubiquitin-Protein Ligases)
EC 2.7.10.1 (EPHB2 protein, human)
تواريخ الأحداث: Date Created: 20240130 Date Completed: 20240131 Latest Revision: 20240325
رمز التحديث: 20240325
مُعرف محوري في PubMed: PMC10945567
DOI: 10.7554/eLife.89176
PMID: 38289221
قاعدة البيانات: MEDLINE
الوصف
تدمد:2050-084X
DOI:10.7554/eLife.89176