Academic Journal

Ca

التفاصيل البيبلوغرافية
العنوان: Ca
المؤلفون: Zheng, Qiaoxia, Zhang, Huan, Zhao, Hongyu, Chen, Yong, Yang, Hongzhining, Li, Tingting, Cai, Qixu, Chen, Yingyu, Wang, Youjun, Zhang, Mingjie, Zhang, Hong
المصدر: Mol Cell ; ISSN:1097-4164
بيانات النشر: Elsevier Science
سنة النشر: 2024
المجموعة: PubMed Central (PMC)
مصطلحات موضوعية: Ca(2+) transient, CaMKIIβ, FIP200, autophagosome, liquid-liquid phase separation
الوصف: In multicellular organisms, very little is known about how Ca2+ transients on the ER outer surface elicited by autophagy stimuli are sustained and decoded to trigger autophagosome formation. Here, we show that Ca2+/calmodulin-dependent protein kinase II β (CaMKIIβ) integrates ER Ca2+ transients to trigger liquid-liquid phase separation (LLPS) of the autophagosome-initiating FIP200 complex. In response to ER Ca2+ transients, CaMKIIβ is recruited from actin filaments and forms condensates, which serve as sites for the emergence of or interaction with FIP200 puncta. CaMKIIβ phosphorylates FIP200 at Thr269, Thr1127, and Ser1484 to modulate LLPS and properties of the FIP200 complex, thereby controlling its function in autophagosome formation. CaMKIIβ also controls the amplitude, duration, and propagation of ER Ca2+ transients during autophagy induction. CaMKIIβ mutations identified in the neurodevelopmental disorder MRD54 affect the function of CaMKIIβ in autophagy. Our study reveals that CaMKIIβ is essential for sustaining and decoding ER Ca2+ transients to specify autophagosome formation in mammalian cells.
نوع الوثيقة: article in journal/newspaper
اللغة: English
Relation: https://doi.org/10.1016/j.molcel.2024.12.005; https://pubmed.ncbi.nlm.nih.gov/39742665
DOI: 10.1016/j.molcel.2024.12.005
الاتاحة: https://doi.org/10.1016/j.molcel.2024.12.005
https://pubmed.ncbi.nlm.nih.gov/39742665
Rights: Copyright © 2024 Elsevier Inc. All rights reserved.
رقم الانضمام: edsbas.3A375E7C
قاعدة البيانات: BASE
الوصف
DOI:10.1016/j.molcel.2024.12.005