Regulation of LRRK2: insights from structural and biochemical analysis.
Autor: | Gilsbach BK; DZNE-German Center for Neurodegenerative Diseases, Otfried-Müller Str. 23, D-72076 Tübingen, Germany., Eckert M; DZNE-German Center for Neurodegenerative Diseases, Otfried-Müller Str. 23, D-72076 Tübingen, Germany., Gloeckner CJ; DZNE-German Center for Neurodegenerative Diseases, Otfried-Müller Str. 23, D-72076 Tübingen, Germany.; University of Tübingen, Institute for Ophthalmic Research, Center for Ophthalmology, Elfriede-Aulhorn-Str. 7, D-72076 Tübingen, Germany. |
---|---|
Jazyk: | angličtina |
Zdroj: | Biological chemistry [Biol Chem] 2018 Jun 27; Vol. 399 (7), pp. 637-642. |
DOI: | 10.1515/hsz-2018-0132 |
Abstrakt: | Leucine-rich repeat kinase 2 (LRRK2) is a multi-domain protein and its mutations can lead to Parkinson's disease. Recent studies on LRRK2 and homologue proteins have advanced our mechanistic understanding of LRRK2 regulation. Here, we summarize the available data on the biochemistry and structure of LRRK2 and postulate three possible layers of regulation, translocation, monomer-dimer equilibrium and intramolecular activation of domains. |
Databáze: | MEDLINE |
Externí odkaz: |