+ |
MAP1LC3C | up-regulates activity
binding
|
ATG3 |
0.773 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-191552 |
|
|
Mus musculus |
MEF Cell |
pmid |
sentence |
22170151 |
Lc3-i is activated by the same atg7 involved in atg12 conjugation, transferred to atg3, a second e2-like enzyme, and finally conjugated to pe |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Pathways: | Autophagy |
+ |
ATG4B | up-regulates activity
cleavage
|
MAP1LC3C |
0.748 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-125489 |
|
|
Homo sapiens |
HEK-293 Cell, HeLa Cell |
pmid |
sentence |
15187094 |
Human atg4 homologues cleave the carboxyl termini of the three human atg8 homologues, microtubule-associated protein light chain 3 (lc3), gabarap, and gate-16. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Autophagy |
+ |
MAP1LC3C | down-regulates
binding
|
NBR1 |
0.546 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184258 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19250911 |
We performed glutathione s-transferase (gst) pull-down assays using extracts from hek293 cells overexpressing an ha-tagged nbr1(d50r) mutant, which lacks the ability to bind p62 (lamark et al., 2003) (figures s1a and s1b, available online), and gst fusions of six human atg8 homologs: gabarap, gabarapl1, gabarapl2, lc3a, lc3b, and lc3c. Indeed, nbr1 interacted with all these members of the mammalian atg8 protein family. . downregulation of either lc3 or gabarap (or both) family members leads to stabilization and p62-dependent aggregation of nbr1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ATG7 | up-regulates activity
binding
|
MAP1LC3C |
0.781 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-191540 |
|
|
Mus musculus |
|
pmid |
sentence |
22170151 |
Lc3-i is activated by the same atg7 involved in atg12 conjugation, transferred to atg3, a second e2-like enzyme, and finally conjugated to pe |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Pathways: | Autophagy |
+ |
MAP1LC3C | up-regulates
|
Autophagosome_formation |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-219399 |
|
|
Homo sapiens |
|
pmid |
sentence |
20921139 |
We assessed both conversion of LC3-I to its cleaved and lipidated form LC3-II and its translocation to autophagic structures, two steps in autophagosome formation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Fibroma Cell |
Pathways: | Autophagy |
+ |
TP53INP1 | up-regulates
binding
|
MAP1LC3C |
0.283 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-196676 |
|
|
Homo sapiens |
|
pmid |
sentence |
22421968 |
These data indicate that cell death observed after tp53inp1-lc3 interaction depends on both autophagy and caspase activity. We conclude that tp53inp1 could act as a tumor suppressor by inducing cell death by caspase-dependent autophagy. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAP1LC3C | up-regulates activity
binding
|
WDFY3 |
0.612 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266795 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
24668264 |
Here, we show that ALFY binds selectively to LC3C and the GABARAPs through a LIR in its WD40 domain. Binding of ALFY to GABARAP is indispensable for its recruitment to LC3B-positive structures and, thus, for the clearance of certain p62 structures by autophagy. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |