Autor: |
Ravi K. Nookala, Lars Langemeyer, Angela Pacitto, Bernardo Ochoa-Montaño, Jane C. Donaldson, Beata K. Blaszczyk, Dimitri Y. Chirgadze, Francis A. Barr, J. Fernando Bazan, Tom L. Blundell |
Jazyk: |
angličtina |
Rok vydání: |
2012 |
Předmět: |
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Zdroj: |
Open Biology, Vol 2, Iss 8 (2012) |
Druh dokumentu: |
article |
ISSN: |
2046-2441 |
DOI: |
10.1098/rsob.120071 |
Popis: |
Mutations in the renal tumour suppressor protein, folliculin, lead to proliferative skin lesions, lung complications and renal cell carcinoma. Folliculin has been reported to interact with AMP-activated kinase, a key component of the mammalian target of rapamycin pathway. Most cancer-causing mutations lead to a carboxy-terminal truncation of folliculin, pointing to a functional importance of this domain in tumour suppression. We present here the crystal structure of folliculin carboxy-terminal domain and demonstrate that it is distantly related to differentially expressed in normal cells and neoplasia (DENN) domain proteins, a family of Rab guanine nucleotide exchange factors (GEFs). Using biochemical analysis, we show that folliculin has GEF activity, indicating that folliculin is probably a distantly related member of this class of Rab GEFs. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
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