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GTP binding controls complex formation by the human ROCO protein MASL1.

Dihanich, S; Civiero, L; Manzoni, C; Mamais, A; Bandopadhyay, R; Greggio, E; Lewis, PA; (2014) GTP binding controls complex formation by the human ROCO protein MASL1. FEBS J , 281 (1) pp. 261-274. 10.1111/febs.12593. Green open access


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The human ROCO proteins are a family of multi-domain proteins sharing a conserved ROC-COR supra-domain. The family has four members: leucine-rich repeat kinase 1 (LRRK1), leucine-rich repeat kinase 2 (LRRK2), death-associated protein kinase 1 (DAPK1) and malignant fibrous histiocytoma amplified sequences with leucine-rich tandem repeats 1 (MASL1). Previous studies of LRRK1/2 and DAPK1 have shown that the ROC (Ras of complex proteins) domain can bind and hydrolyse GTP, but the cellular consequences of this activity are still unclear. Here, the first biochemical characterization of MASL1 and the impact of GTP binding on MASL1 complex formation are reported. The results demonstrate that MASL1, similar to other ROCO proteins, can bind guanosine nucleotides via its ROC domain. Furthermore, MASL1 exists in two distinct cellular complexes associated with heat shock protein 60, and the formation of a low molecular weight pool of MASL1 is modulated by GTP binding. Finally, loss of GTP enhances MASL1 toxicity in cells. Taken together, these data point to a central role for the ROC/GTPase domain of MASL1 in the regulation of its cellular function.

Type: Article
Title: GTP binding controls complex formation by the human ROCO protein MASL1.
Open access status: An open access version is available from UCL Discovery
DOI: 10.1111/febs.12593
Publisher version: http://dx.doi.org/10.1111/febs.12593
Additional information: © 2013 The Authors. FEBS Journal published by John Wiley & Sons Ltd on behalf of FEBS 261 This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Keywords: ROCO, G-protein, HSP60, LRRK2, MASL1, complex formation
URI: http://discovery.ucl.ac.uk/id/eprint/1415947
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