| + |
BAG5 | down-regulates activity 
binding
|
HSPA1B |
0.661 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261197 |
|
|
Homo sapiens |
Brain |
| pmid |
sentence |
| 15603737 |
Here, we show that BAG5, a BAG domain-containing family member, interacts with both Hsp70 and parkin with deleterious functional consequences. Through these interactions, BAG5 inhibits Hsp70 chaperone activity and parkin E3 ubiquitin ligase activity; Thus, BAG5 interacts with Hsp70 in vitro and in vivo, and substitution of select residues within the BAG domains is sufficient to abolish this interaction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BAG5 | down-regulates activity
binding
|
PRKN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261198 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15603737 |
Here, we show that BAG5, a BAG domain-containing family member, interacts with both Hsp70 and parkin with deleterious functional consequences. Through these interactions, BAG5 inhibits Hsp70 chaperone activity and parkin E3 ubiquitin ligase activity Immunoprecipitation (IP) of GFP-parkin resulted in the coimmunoprecipitation of both Hsp70 and BAG5 or BAG5(DARA) (Figure 4A). Furthermore, IP of GFP-parkin resulted in the coimmunoprecipitation of BAG5 or BAG5 (DARA) in the absence of overexpressed Hsp70. Taken together, these data demonstrate that BAG5 can directly inhibit parkin-mediated autoubiquitinylation independently of Hsp70. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BAG5 | down-regulates activity
binding
|
HSPA1A |
0.736 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261196 |
|
|
Homo sapiens |
Brain |
| pmid |
sentence |
| 15603737 |
Here, we show that BAG5, a BAG domain-containing family member, interacts with both Hsp70 and parkin with deleterious functional consequences. Through these interactions, BAG5 inhibits Hsp70 chaperone activity and parkin E3 ubiquitin ligase activity; Thus, BAG5 interacts with Hsp70 in vitro and in vivo, and substitution of select residues within the BAG domains is sufficient to abolish this interaction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
BAG5
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