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Chem Biol. 2014 Jul 17;21(7):809-18. doi: 10.1016/j.chembiol.2014.05.010. Epub 2014 Jun 26.

Genetic, structural, and molecular insights into the function of ras of complex proteins domains.

Author information

1
Department of Biology, University of Padova, Via U. Bassi 58/b, Padova 35131, Italy.
2
Department of Molecular Neuroscience, UCL Institute of Neurology, Queen Square, London WC1N 3BG, UK.
3
Department of Molecular Neuroscience, UCL Institute of Neurology, Queen Square, London WC1N 3BG, UK; School of Pharmacy, University of Reading, Whiteknights, Reading RG6 6AP, UK; Centre for Integrated Neuroscience and Neurodynamics, University of Reading, Whiteknights, Reading RG6 6AP, UK. Electronic address: p.a.lewis@reading.ac.uk.
4
Department of Biology, University of Padova, Via U. Bassi 58/b, Padova 35131, Italy. Electronic address: elisa.greggio@unipd.it.

Abstract

Ras of complex proteins (ROC) domains were identified in 2003 as GTP binding modules in large multidomain proteins from Dictyostelium discoideum. Research into the function of these domains exploded with their identification in a number of proteins linked to human disease, including leucine-rich repeat kinase 2 (LRRK2) and death-associated protein kinase 1 (DAPK1) in Parkinson's disease and cancer, respectively. This surge in research has resulted in a growing body of data revealing the role that ROC domains play in regulating protein function and signaling pathways. In this review, recent advances in the structural information available for proteins containing ROC domains, along with insights into enzymatic function and the integration of ROC domains as molecular switches in a cellular and organismal context, are explored.

PMID:
24981771
PMCID:
PMC4104024
DOI:
10.1016/j.chembiol.2014.05.010
[Indexed for MEDLINE]
Free PMC Article

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