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Article Addendum

REI-1, a Novel Rab11 GEF with a SH3BP5 domain

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Article: e1208325 | Received 15 Jun 2016, Accepted 27 Jun 2016, Published online: 15 Aug 2016

Figures & data

Figure 1. (A) Domain structure of the REI-1 family of proteins. Our results show that almost full-length REI-1 (1-228 aa) is required for RAB-11.1 binding. (B) A model describing the role of REI-1 in RAB-11 activation and translocation. REI-1 activates RAB-11, by exchange of GDP with GTP, principally at late-Golgi membranes. RAB-11-positive post-Golgi vesicles or compartments are then targeted to the cell cortex and cleavage furrow to regulate cytokinesis and membrane traffic.

Figure 1. (A) Domain structure of the REI-1 family of proteins. Our results show that almost full-length REI-1 (1-228 aa) is required for RAB-11.1 binding. (B) A model describing the role of REI-1 in RAB-11 activation and translocation. REI-1 activates RAB-11, by exchange of GDP with GTP, principally at late-Golgi membranes. RAB-11-positive post-Golgi vesicles or compartments are then targeted to the cell cortex and cleavage furrow to regulate cytokinesis and membrane traffic.