| + |
FBXO27 | down-regulates quantity by destabilization 
binding
|
LAMP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272323 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28743755 |
Here, we report the characterization of FBXO27, a glycoprotein-specific F-box protein that is part of the SCF (SKP1/CUL1/F-box protein) ubiquitin ligase complex, and demonstrate that SCFFBXO27 ubiquitinates glycoproteins in damaged lysosomes to regulate autophagic machinery recruitment.We found that the lysosomal protein LAMP2, which is ubiquitinated preferentially on lysosomal damage, enhances autophagic machinery recruitment to damaged lysosomes. Thus, we propose that SCFFBXO27 ubiquitinates glycoproteins exposed upon lysosomal damage to induce lysophagy. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXO27 | up-regulates activity 
binding
|
Cullin 1-RBX1-Skp1 |
0.658 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272325 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28743755 |
Here, we report the characterization of FBXO27, a glycoprotein-specific F-box protein that is part of the SCF (SKP1/CUL1/F-box protein) ubiquitin ligase complex, and demonstrate that SCFFBXO27 ubiquitinates glycoproteins in damaged lysosomes to regulate autophagic machinery recruitment.We found that the lysosomal protein LAMP2, which is ubiquitinated preferentially on lysosomal damage, enhances autophagic machinery recruitment to damaged lysosomes. Thus, we propose that SCFFBXO27 ubiquitinates glycoproteins exposed upon lysosomal damage to induce lysophagy. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
FBXO27
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