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NMR characterisation of the minimal interacting regions of centrosomal proteins 4.1R and NuMA1: effect of phosphorylation
|Authors:||Treviño, Miguel A. ; Rodríguez Rodríguez, Mar; Correas, Isabel ; Marcilla, Miguel; Albar, Juan Pablo; Rico, Manuel ; Jiménez, M. Angeles ; Bruix, M.|
|Citation:||BMC Biochemistry 11 : 7 (2010)|
|Abstract:||[Background] Some functions of 4.1R in non-erythroid cells are directly related with its distinct sub-cellular
localisation during cell cycle phases. During mitosis, 4.1R is implicated in cell cycle progression and spindle pole
formation, and co-localizes with NuMA1. However, during interphase 4.1R is located in the nucleus and only
partially co-localizes with NuMA1.|
[Results] We have characterized by NMR the structural features of the C-terminal domain of 4.1R and those of the minimal region (the last 64 residues) involved in the interaction with NuMA1. This subdomain behaves as an intrinsically unfolded protein containing a central region with helical tendency. The specific residues implicated in the interaction with NuMA1 have been mapped by NMR titrations and involve the N-terminal and central helical regions. The segment of NuMA1 that interacts with 4.1R is phosphorylated during mitosis. Interestingly, NMR data indicates that the phosphorylation of NuMA1 interacting peptide provokes a change in the interaction mechanism. In this case, the recognition occurs through the central helical region as well as through the C-terminal region of the subdomain meanwhile the N-terminal region do not interact.
[Conclusions] These changes in the interaction derived from the phosphorylation state of NuMA1 suggest that phosphorylation can act as subtle mechanism of temporal and spatial regulation of the complex 4.1R-NuMA1 and therefore of the processes where both proteins play a role.
|Description:||12 pages, 8 figures.|
|Publisher version (URL):||http://dx.doi.org/10.1186/1471-2091-11-7|
|Appears in Collections:||(IQFR) Artículos|