PMC:5026484 / 14430-15873 JSONTXT

{"target":"http://pubannotation.org/docs/sourcedb/PMC/sourceid/5026484","sourcedb":"PMC","sourceid":"5026484","source_url":"https://www.ncbi.nlm.nih.gov/pmc/5026484","text":"10.7554/eLife.18675.008Figure 3. Prenylated EHBP1 and EHBP1L1 colocalize with Rab8 and Rab10.\n(a) EHBP1 and EHBP1L1 can be prenylated in vitro as shown by mass spectrometry. After incubation of the purified proteins including the CaaX-motifs (theoretical masses of the purified proteins: 22253.3 Da (EHBP1); 22214.0 Da (EHBP1L1); left panel) with Farnesytransferase (FTase, middle panel) or Geranylgeranyltransferase (GGTase, right panel) farnesylation/geranylgeranylation lead to an increase in mass of 205.4/272.5 Da, respectively. Note that farnesylation, in contrast to geranylgeranylation, appears to be more efficient under similar conditions and goes to completion. This is in agreement with the sequence of the CaaX-motifs in both proteins containing a Gln/Ser at their C-terminus which has been shown to favor farnesylation. (b) Whereas the constructs containing the bMERB domain and the CaaX-motif (EHBP11047-1231, EHBP1L11340-1523) localize to intracellular structures resembling endosomes, deletion of the CaaX-motif (∆CaaX) leads to a cytosolic distribution for both EHBP1 and EHBP1L1 (Scale bars: 10 µm). (c) Both EGFP-EHBP11047-1231 and EGFP-EHBP1L11340-1523 (upper panel) show strong colocalisation with mCherry-Rab8Q67L and mCherry-Rab10Q68L (middle panel) as indicated in the merged images (lower panel). The localization pattern resembles that of endosomes (Scale bars: 10 µm).\nDOI: http://dx.doi.org/10.7554/eLife.18675.008","divisions":[{"label":"Title","span":{"begin":33,"end":93}}],"tracks":[]}