protein
| interacting with FOXO3 (FOXO3 controls the transcription of autophagy-related genes, including MAP1LC3 and BNIP3 |
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MAP1LC3A is a novel regulatory protein interacting with AKAP13 |
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FYCO1 binds to both MAP1LC3A, PtdIns(3)P and RAB7A, and contains a domain responsible for microtubule plus end-dependent transport |
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MAP1S isoforms may act as a linker to bridge autophagy components not only with the microtubular cytoskeleton through interacting with MAP1LC3A isoforms, but also directly to mitochondria |
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hypoxia induced dephosphorylation of FUNDC1 and enhanced its interaction with MAP1LC3A for selective mitophagy |
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strong evidence that transcriptional repression plays a major role in regulating Atg8/LC3 levels, and this up-regulation results in an increase in the size of the autophagosome |
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ULK1 interacted most strongly with GABARAP and GABARAPL1, but it also interacted with GABARAPL2, MAP1LC3A, and MAP1LC3C |
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although AP2 and PICALM bind to MAP1LC3A, they do not seem to be direct substrates of autophagy |
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interaction between MAP1LC3A and AP2M1 as well as PICALM showed a significant increase triggered by starvation |
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at mitochondria, ULK1 interacts with FUNDC1, phosphorylating it at serine 17, which enhances FUNDC1 binding to MAP1LC3A |
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DACT1 increases autophagosome formation as indicated by elevated puncta formation of MAP1LC3A, ATG14 and ZFYVE1 (Double FYVE-containing protein 1) |
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LRPPRC interacts with MAP1S that interacts with MAP1LC3A and bridges autophagy components with microtubules and mitochondria to affect autophagy flux |
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AMBRA1 is able to induce mitophagy via MAP1LC3A binding, regardless of PARK2 and SQSTM1 |
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autophagy protein MAP1LC3A/Atg8 directly interacts with the nuclear lamina protein LMNB1 (lamin B1), and binds to LMN/lamin-associated chromatin domains (LADs) |
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FUNDC1, mediate selective removal of damaged or superfluous mitochondria through their specific interaction with MAP1LC3A |
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GABARAP subfamily members, GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3B, are primary contributors to PINK1/Parkin mitophagy and starvation autophagy |
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KLC1 may potentially compete with MAP1LC3A, a key component for autophagosome formation, to interact with FUNDC1 |
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FKBP8 efficiently recruits lipidated MAP1LC3A to damaged mitochondria in a LIR-dependent manner |