Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1773, Issue 11, Pages 1628-1636Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2007.07.013
Keywords
CacyBP/SIP; tubulin; interaction; differentiation; globular assemblies; NB2a cells
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CacyBP/SIP, originally identified as a S100A6 (calcyclin) target, was later shown to interact with some other members of the S 100 family as well as with Siah-1 and Skp 1 proteins. Recently, it has been shown that CacyBP/SLP is up-regulated during differentiation of cardiomyocytes. In this work we show that the level of CacyBP/SlP is higher in differentiated neuroblastoma NB2a cells than in undifferentiated ones and that in cells overexpressing CacyBP/SIP the level of GAP-43, a marker of differentiation, was increased. Since the process of differentiation is accompanied by an extensive rearrangement of microtubules, we examined whether CacyBP/SlP interacted with tubulin. By applying cross-linking experiments we found that these two proteins bind directly. The dissociation constant of the tubulin-CacyBP/SIP complex determined by the surface plasmon resonance technique is 1.57 x 10(-7) M which suggests that the interaction is tight. The interaction and co-localization of CacyBP/SIP and tubulin was also demonstrated by co-immunoprecipitation, affinity chromatography and immunofluorescence methods. Light scattering measurements and electron microscopy studies revealed that CacyBP/SIP, but not its homologue, Sgt1, increased tubulin oligomerization. Altogether, our results suggest that CacyBP/SIP, via its interaction with tubulin, might contribute to the differentiation of neuroblastoma NB2a cells. (C) 2007 Elsevier B.V. All rights reserved.
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