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. 2001 Apr 16;153(2):351–366. doi: 10.1083/jcb.153.2.351

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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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Identification of proteins interacting with the SH3 domain of Abp1. (a) Blot overlay analysis using a GST-fusion protein containing the COOH-terminal half of Abp1 onto different rat tissue homogenates identified several bands prominent in brain at 75/80, 100, 145, and 180 kD. (b) Blot overlay analysis using a GST-fusion protein of the SH3 domain revealed bands of similar molecular weights not only in brain but in part also in testis and lung. (c) Affinity purifications of proteins interacting with the SH3 domains of Abp1, endophilin I, and syndapin I. Equal amounts of fusion proteins and brain extracts (0.625 mg brain protein per pull down) were used. 12.45 μg of starting material (corresponding to 1/50) were loaded for comparison. (d) Immunoprecipitated dynamin (arrow) was detected by both antidynamin antibodies (left) and by the Abp1-SH3 domain (right). Left two lanes in each gel: IP buffer with 150 mM salt; right two lanes in each gel: IP buffer with 100 mM salt.