The dynamic Rab11-FIPs

Molecular Cell Biology Laboratory, Department of Biochemistry, Biosciences Institute, University College Cork, Cork, Ireland.
Biochemical Society Transactions (Impact Factor: 3.19). 10/2009; 37(Pt 5):1032-6. DOI: 10.1042/BST0371032
Source: PubMed


The Rab11-FIPs (Rab11-family interacting proteins; also known as FIPs) constitute an evolutionarily conserved protein family that act as effector molecules for multiple Rab and Arf (ADP-ribosylation factor) GTPases. They were initially characterized by their ability to bind Rab11 subfamily members via a highly-conserved C-terminal RBD (Rab11-binding domain). Resolution of the crystal structure of Rab11 in complex with FIPs revealed that the RBD mediates homodimerization of the FIP molecules, creating two symmetrical interfaces for Rab11 binding and leading to the formation of a heterotetrameric complex between two FIP and two Rab11 molecules. The FIP proteins are encoded by five genes and alternative splicing has been reported. Based on primary structure, the FIPs were subcategorized into two classes: class I [Rip11, FIP2 and RCP (Rab-coupling protein)] and class II (FIP3 and FIP4). Recent studies have identified the FIPs as key players in the regulation of multiple distinct membrane trafficking events. In this mini-review, we summarize the Rab11-FIP field and discuss, at molecular and cellular levels, the recent findings on FIP function.

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    • "An 85-amino-acid (aa) intracellular juxtamembrane region of the TrkB receptor was selected as bait, since the region was shown to be important for endocytic TrkB recycling (Chen et al., 2005; Huang et al., 2009). Among the positive clones was Rab11-FIP3, a protein that has been also established to interact with ADP-ribosylation factors (ARF5, ARF6) as well as with motor proteins (kinesin I, dynein light intermediate chain) (Horgan et al., 2010; Prekeris, 2003; Simon and Prekeris, 2008), and was previously shown to modulate recycling of various cargoes (Horgan and McCaffrey, 2009; Prekeris, 2003). We confirmed with co-immunoprecipitation studies that Rab11-FIP3 and TrkB receptors interacted (Figure S5A). "
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    Developmental Cell 05/2015; 33(6). DOI:10.1016/j.devcel.2015.04.009 · 9.71 Impact Factor
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    • "These phospholipids are known to affect membrane trafficking in post-Golgi and recycling membrane compartments (De Matteis et al., 2005). Another potential substrate, Rab11fip5, is a member of Rab11 family interacting proteins (Horgan and McCaffrey, 2009), which could affect membrane trafficking from recycling endosomes in dendrites (Wang et al., 2008). "
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