Orchestration of autophagosome fusion by STRIPAK complex components in muscle tissue
Autophagy is a central process responsible for the disposal of normal as well as damaged cellular proteins and organelles. Proper regulation of multiple steps – including initiation and the fusion between autophagosomes and lysosomes – is essential for the completion of cargo disposal. While the fun...
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Published in | Autophagy reports Vol. 2; no. 1 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Taylor & Francis Group
31.12.2023
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Subjects | |
Online Access | Get full text |
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Summary: | Autophagy is a central process responsible for the disposal of normal as well as damaged cellular proteins and organelles. Proper regulation of multiple steps – including initiation and the fusion between autophagosomes and lysosomes – is essential for the completion of cargo disposal. While the function of many proteins that mediate canonical autophagy has been characterized, the identification of new autophagy regulators may shed light on differences between tissues and/or responses to cellular stresses. In this punctum, we discuss our recent findings about how the Striatin-Interacting Phosphatase and Kinase (STRIPAK)-NUAK-Starvin (Stv) complex coordinately regulates autophagy in the muscle tissue of Drosophila melanogaster. Abbreviations: Atg8a, autophagy-related 8a; BAG3, BCL2–associated athanogene 3; CASA, chaperone-assisted selective autophagy; Cp1, Cysteine proteinase-1; Fgop2, fibroblast growth factor receptor 1 oncogene partner 2; FLNC, Filamin C; HSC70, heat-shock cognate 70 complex; Mob4, MOB kinase activator 4; PLA, proximity ligation assay; Rab7, ras-related protein rab-7; RNAi, RNA interference; Strip, striatin-interacting protein; STRIPAK, striatin interacting phosphatase and kinase; Stv, starvin; SQSTM1, sequestosome 1; TFEB, transcription factor EB; Ub, ubiquitin. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 2769-4127 2769-4127 |
DOI: | 10.1080/27694127.2023.2260670 |