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. 2001 Apr 30;153(3):585–598. doi: 10.1083/jcb.153.3.585

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© 2001 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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A point mutation that disrupts the ILK binding impairs the FA localization of CH-ILKBP. (A) GST–CH-ILKBP proteins. GST fusion proteins containing the mutant form (F271D) of CH2 domain (residues 258–372) (lane 1), the CH2 domain (residues 258–372) (lane 2), CH-ILKBP (lane 4), and the F271D point mutant (lane 5) and GST (lane 3) were separated on SDS-PAGE (10 μg/lane) and detected by Coomassie blue R-250 staining. (B) ILK binding. C2C12 cell lysates (260 μg) were incubated and precipitated with equal amount (10 μg) of GST or GST–CH-ILKBP proteins as indicated. ILK was detected by Western blotting with anti-ILK antibody 65.1. Lane 1 was loaded with C2C12 cell lysates (9 μg/lane). (C and D) FA localization. Rat mesangial cells expressing GFP fusion protein containing the full-length F271D point mutant were plated on fibronectin-coated coverslips and stained with anti-ILK antibody 65.1 and Rhodamine red™-conjugated anti–mouse IgG antibody. GFP-F271D (C) and ILK (D) were visualized under a fluorescence microscope equipped with GFP and rhodamine filters. Bar, 5 μm.