JCS02599 Supplementary Material

Files in this Data Supplement:

• Supplemental Figure 1 - Fig. S1. Amino acid sequence alignment of specific domains of the Mon2 protein family. The sequence of the A domain (from residue 10 to 52) (A) and the F domain (from residue 1524 to 1636) (B) of Mon2p are aligned with the sequence of conserved domains of proteins described in Fig.1A. The approximately 100%, 80% and 60% conserved residues are highlighted in black, dark grey and light grey, respectively. The black bars above the alignments indicate predicted a-helices.

• Supplemental Figure 2 - Fig. S2. Amino acid sequence alignment of conserved domains of Mon2p present in the large Sec7 GEFs. The sequence of the B domain (from amino acid residues 53 to 178). (A) and C domain (from amino acid residues 204 to 380) (B) of Mon2p are aligned with the conserved domains of proteins described in Fig. 1, using the representation indicated in Fig. S1. The grey bar indicates a predicted loop containing the Y-D motif in a conserved region described by (Jackson and Casanova, 2000).

• Supplemental Figure 3 - Fig. S3. PM- or endosome-to-Golgi recycling transport defects in the Dmon2 mutant become evident at high temperature. (A) GFP-Snc1p (Lewis et al., 2000) no longer displays its characteristic localization to the PM and intracellular punctate in the Dmon2 mutant at 37°C. (B) Similarly, but to a lesser extent, GFP-Tlg2p (J.A.E., unpublished) also becomes more cytosolic in the mutant.

  Reference

  Lewis, M. J., Nichols, B. J., Prescianotto-Baschong, C., Riezman, H., and Pelham, H. R. (2000). Specific retrieval of the exocytic SNARE Snc1p from early yeast endosomes. Mol. Biol. Cell 11, 23-38.