The ubiquitin ligase E6-AP (E6-associated protein) represents a prime example for the notion that deregulated modification of proteins with ubiquitin contributes to the development of human disease: loss of E6-AP function by mutation is responsible for the development of AS (Angelman syndrome), a neurological disorder, and unscheduled activation of E6-AP by complex formation with the E6 oncoprotein of HPVs (human papillomaviruses) contributes to cervical carcinogenesis. However, while there is a considerable amount of data concerning the oncogenic properties of the E6–E6-AP complex, only little is known about the function(s) of E6-AP in neurons. This is mainly due to the fact that although some E6-AP substrates have been identified, it is at present unclear whether deregulated modification/degradation of these proteins is involved in the pathogenesis of AS. Similarly, the cellular pathways involving E6-AP remain enigmatic. To obtain insights into the physiological functions of E6-AP, we are currently employing several strategies, including quantitative affinity proteomics and RNA interference approaches. The results obtained will eventually allow the introduction of E6-AP into functional protein networks and so reveal potential targets for molecular approaches in the treatment of E6-AP-associated diseases.
Skip Nav Destination
Article navigation
October 2008
-
Cover Image
Cover Image
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
Conference Article|
September 19 2008
Ubiquitin ligase E6-AP and its role in human disease
Konstantin Matentzoglu;
Konstantin Matentzoglu
*Laboratory of Cellular Biochemistry, Department of Biology, University of Konstanz, 78457 Konstanz, Germany
Search for other works by this author on:
Martin Scheffner
Martin Scheffner
1
*Laboratory of Cellular Biochemistry, Department of Biology, University of Konstanz, 78457 Konstanz, Germany
†Konstanz Research School Chemical Biology, University of Konstanz, 78457 Konstanz, Germany
1To whom any correspondence should be addressed (email [email protected]).
Search for other works by this author on:
Publisher: Portland Press Ltd
Received:
March 06 2008
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2008 Biochemical Society
2008
Biochem Soc Trans (2008) 36 (5): 797–801.
Article history
Received:
March 06 2008
Citation
Konstantin Matentzoglu, Martin Scheffner; Ubiquitin ligase E6-AP and its role in human disease. Biochem Soc Trans 1 October 2008; 36 (5): 797–801. doi: https://doi.org/10.1042/BST0360797
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.
Biochemical Society Member Sign in
Sign InSign in via your Institution
Sign in via your InstitutionGet Access To This Article
Get Email Alerts
Open Access for all
We offer compliant routes for all authors from 2025. With library support, there will be no author nor reader charges in 5 journals. Check here |
![]() |