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. 2014 Aug 19;14:78. doi: 10.1186/s12935-014-0078-8

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Copyright © 2014 Aljaberi et al.; licensee Springer

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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K129E reduces the affinity of survivin for borealin. (A) HeLa cells expressing WT or K129E (green), depleted of endogenous survivin were fixed with formaldehyde and probed to localise borealin (red) at the centromeres of prometaphase cells or (B) at the anaphase spindle. (C) Immunoblot of borealin co-immunoprecipitated with anti-GFP antibodies from lysates prepared from cells ectopically expressing GFP, WT or K129E. (D-F) 3D ribbon models of survivin (grey) bound to the NH₂ terminus of borealin (black) constructed from structure 2RAW using UCSF Chimera [20]. K129 and its side chain are highlighted in red. (E, F) Magnified and rotated models of the C-terminus of survivin bound to borealin from (D), with the side chain of D29 of borealin (black), and (F) an upstream glutamic acid (E125^svn) indicated in blue mesh to demonstrate how this charge change could affect the proximity of K129^svn (red mesh) and D29^bor (black mesh).