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. 1999 Dec 13;147(6):1275–1286. doi: 10.1083/jcb.147.6.1275

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© 1999 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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Association of ACF7 COOH-terminal domain with MTs. Transient transfections of pFLAG-mACF7-C (A–D) and pFLAG-ABD (E and F) were performed in COS-7 cells. Transfected cells were stained with monoclonal anti-FLAG M2 antibody (A, C, and E), polyclonal anti–Tyr-tubulin antibody (B), polyclonal anti–Glu-tubulin antibody (D), and polyclonal antitubulin antibody (F), and were examined by immunofluorescence microscopy. mACF7-C proteins colocalize with most of the Tyr-MTs (A and B) and all of the Glu-MTs (C and D). The noncolocalized Tyr-MTs are indicated by an arrow (B). Frequently, long MTs forming whorls were observed in pFLAG–mACF7-C transfected cells (B and D). The overexpressed ABD protein did not associate with the MT network (E and F). Bar, 20 μm.