protein
| interacts with tubulin and GABA(A) receptor |
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ATG4B displays increased activity against GABARAPL1 |
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interacting with STBD1, and AIM in STBD1 is responsible for its interaction with GABARAPL1 |
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HSP90AA1 interacts and protects GABARAPL1 from its degradation by the proteasome |
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strong evidence that transcriptional repression plays a major role in regulating GARAPL1/MAP1LC3A levels, and this up-regulation results in an increase in the size of the autophagosome |
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MAP1LC3B, GABARAP and GABARAPL1 are novel interactors of MAPK15, a MAP kinase involved in cell proliferation and transformation |
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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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TBC1D5 controls cellular endomembrane trafficking processes and binds the retromer subunit VPS29 and the ubiquitin-like protein GABARAPL1 |
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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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FKBP8 is an GABARAPL1, GABARAPL2-interacting protein |
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ATG4B, a key enzyme in autophagy that cleaves GABARAPL1, is an interactor of the small GTPase RAB7B |
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ATG7 recognizes GABARAPL1, GARAPL2 through multiple steps, which would be necessary to induce a conformational change in ATG7 that is optimal for the activation reaction |
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novel function of GABARAPL1 to activate TFEB, a master transcription factor of autophagy and lysosome function during lysosomal damage |