BACKGROUND INFORMATION: Rab11 and Rab14 are two related Rab GTPases that are believed to function in endosomal recycling and Golgi/endosome transport processes. We, and others, have identified a group of proteins that interact with Rab11 and function as Rab11 effectors, known as the Rab11-FIPs (family interacting proteins). This protein family has been sub-classified into two groups - class I FIPs [FIP2, RCP (Rab coupling protein) and Rip11 (Rab11-interacting protein)] and class II FIPs (FIP3 and FIP4). RESULTS: In the present study we identify the class I FIPs as dual Rab-binding proteins by demonstrating that they also interact with Rab14 in a GTP-dependent manner. We show that these interactions are specific for the class I FIPs and that they occur via their C-terminal regions, which encompass the previously described RBD (Rab11-binding domain). Furthermore, we show that Rab14 significantly co-localizes with the TfnR (transferrin receptor) and that Rab14 Q70L co-localizes with Rab11a and with the class I FIPs on the ERC (endosomal recycling compartment) during interphase. Additionally, we show that during cytokinesis Rab14 localizes to the cleavage furrow/midbody. CONCLUSIONS: The data presented in the present study, which identifies the class I FIPs as the first putative effector proteins for the Rab14 GTPase, indicates greater complexity in the Rab-binding specificity of the class I FIP proteins.
BACKGROUND INFORMATION: Rab11 and Rab14 are two related Rab GTPases that are believed to function in endosomal recycling and Golgi/endosome transport processes. We, and others, have identified a group of proteins that interact with Rab11 and function as Rab11 effectors, known as the Rab11-FIPs (family interacting proteins). This protein family has been sub-classified into two groups - class I FIPs [FIP2, RCP (Rab coupling protein) and Rip11 (Rab11-interacting protein)] and class II FIPs (FIP3 and FIP4). RESULTS: In the present study we identify the class I FIPs as dual Rab-binding proteins by demonstrating that they also interact with Rab14 in a GTP-dependent manner. We show that these interactions are specific for the class I FIPs and that they occur via their C-terminal regions, which encompass the previously described RBD (Rab11-binding domain). Furthermore, we show that Rab14 significantly co-localizes with the TfnR (transferrin receptor) and that Rab14Q70L co-localizes with Rab11a and with the class I FIPs on the ERC (endosomal recycling compartment) during interphase. Additionally, we show that during cytokinesis Rab14 localizes to the cleavage furrow/midbody. CONCLUSIONS: The data presented in the present study, which identifies the class I FIPs as the first putative effector proteins for the Rab14 GTPase, indicates greater complexity in the Rab-binding specificity of the class I FIP proteins.
Authors: Carl Laflamme; Jacob A Galan; Khaled Ben El Kadhi; Antoine Méant; Carlos Zeledon; Sébastien Carréno; Philippe P Roux; Gregory Emery Journal: Mol Cell Biol Date: 2017-01-19 Impact factor: 4.272
Authors: Patrick Lall; Andrew J Lindsay; Sara Hanscom; Tea Kecman; Elizabeth S Taglauer; Una M McVeigh; Edward Franklin; Mary W McCaffrey; Amir R Khan Journal: J Biol Chem Date: 2015-05-31 Impact factor: 5.157
Authors: Forgivemore Magunda; Chelsea Wright Thompson; David A Schneider; Susan M Noh Journal: Appl Environ Microbiol Date: 2016-07-15 Impact factor: 4.792
Authors: Junghwa Kirschman; Mingli Qi; Lingmei Ding; Jason Hammonds; Krista Dienger-Stambaugh; Jaang-Jiun Wang; Lynne A Lapierre; James R Goldenring; Paul Spearman Journal: J Virol Date: 2018-02-12 Impact factor: 5.103
Authors: Sam E Reed; Lorna R Hodgson; Shuang Song; Margaret T May; Eoin E Kelly; Mary W McCaffrey; Cynthia C Mastick; Paul Verkade; Jeremy M Tavaré Journal: J Cell Sci Date: 2013-02-26 Impact factor: 5.285