QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

Help viewing high resolution images Return to article

Fig. 4. Optimal interaction of TOM1 with clathrin involves three sites: residues 300-321, 321-326 and 362-366. (A) Schematic diagram of TOM1 C-terminal deletion constructs used in the clathrin pull-down experiments. The relative efficiency with which each construct pulled down clathrin as observed in B is indicated on the right as + or -. (B) The clathrin-binding domain of TOM1 includes one putative clathrin-binding box at 321-326, which is sufficient by itself whereas residues 300-321 and 362-366 enhance the clathrin-binding efficiency. The GST fusion constructs shown in A were used to pull down cytosolic clathrin and analyzed as described in Fig. 2B. The upper panels indicate the amounts of clathrin pulled down by 20 µg of GST or GST fusion proteins. Input represents 50 µg of the starting material. The bottom panels are Coomassie-stained versions of the same experiments. (C) Schematic diagram depicting the location of the sites in TOM1 that are critical for optimal clathrin interaction. CB, clathrin-binding site; CB-I and CB-II: clathrin-binding enhancing sites I and II, respectively; EBD, endofin-binding domain; GAT, GGAs and TOM1 homology; VHS, VPS-27, Hrs and STAM.

Return to article