HIF_and_pVHL.png
Size of this preview:
800 × 429 pixels
.
Other resolutions:
320 × 172 pixels
|
640 × 343 pixels
|
1,024 × 549 pixels
|
1,280 × 687 pixels
|
2,560 × 1,374 pixels
|
4,588 × 2,462 pixels
.
|
The categories of this image need checking. You can do so
here
.
|
Summary
| Description |
English:
The regulation of HIF1α by pVHL. Under normal oxygen levels, HIF1α binds pVHL through 2 hydroxylated proline residues and is polyubiquitinated. This leads to its degredation via the proteasome. During hypoxia, the proline residues are not hydroxylated and pVHL cannot bind. HIF1α causes the transcription of genes that contain the hypoxia response element. In VHL disease, genetic mutations cause alterations to the pVHL protein, usually to the HIF1α binding site.
|
| Date | |
| Source | Own work |
| Author | Simon Caulton |
| Other versions |
[
]
|
Info
:
DrTrigonBot
(
talk
) has evaluated this file and left hidden information.
View it!
For a deeper understanding of how the bot works, please consult the
documentation
.
Licensing
I, the copyright holder of this work, hereby publish it under the following license:
This file is licensed under the
Creative Commons
Attribution-Share Alike 3.0 Unported
license.
-
You are free:
- to share – to copy, distribute and transmit the work
- to remix – to adapt the work
-
Under the following conditions:
- attribution – You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use.
- share alike – If you remix, transform, or build upon the material, you must distribute your contributions under the same or compatible license as the original.