Structural highlights
Function
1433S_HUMAN Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity). p53-regulated inhibitor of G2/M progression.
Publication Abstract from PubMed
Binding of 14-3-3 proteins to LRRK2 is known to be impaired by a number of Parkinson's disease (PD)-relevant mutations. Abrogation of this interaction is connected to enhanced LRRK2 kinase activity which in turn is implicated in increased ubiquitination of LRRK2, accumulation of LRRK2 into inclusion bodies and reduction of neurite length. Hence, the interaction between 14-3-3 and LRRK2 is of significant interest as a possible drug target for the treatment of PD. However, LRRK2 possesses multiple sites that upon phosphorylation can bind to 14-3-3, thus rendering the interaction relatively complex. Using biochemical assays and crystal structures, we characterize the multivalent interaction between these two proteins.
Structural interface between LRRK2 and 14-3-3 protein.,Stevers L, de Vries R, Doveston R, Milroy LG, Brunsveld L, Ottmann C Biochem J. 2017 Feb 15. pii: BCJ20161078. doi: 10.1042/BCJ20161078. PMID:28202711[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stevers L, de Vries R, Doveston R, Milroy LG, Brunsveld L, Ottmann C. Structural interface between LRRK2 and 14-3-3 protein. Biochem J. 2017 Feb 15. pii: BCJ20161078. doi: 10.1042/BCJ20161078. PMID:28202711 doi:http://dx.doi.org/10.1042/BCJ20161078
