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. 2013 Mar 21;14(3):6487-98.
doi: 10.3390/ijms14036487.

RUFY, Rab and Rap Family Proteins Involved in a Regulation of Cell Polarity and Membrane Trafficking

Yasuko Kitagishi  1 , Satoru Matsuda
Affiliations

RUFY, Rab and Rap Family Proteins Involved in a Regulation of Cell Polarity and Membrane Trafficking

Yasuko Kitagishi et al. Int J Mol Sci. .

Abstract

Cell survival, homeostasis and cell polarity rely on the control of membrane trafficking pathways. The RUN domain (comprised of the RPIP8, UNC-14, and NESCA proteins) has been suggested to be implicated in small GTPase-mediated membrane trafficking and cell polarity. Accumulating evidence supports the hypothesis that the RUN domain-containing proteins might be responsible for an interaction with a filamentous network linked to actin cytoskeleton and/or microtubules. In addition, several downstream molecules of PI3K are involved in regulation of the membrane trafficking by interacting with vesicle-associated RUN proteins such as RUFY family proteins. In this review, we summarize the background of RUN domain research with an emphasis on the interaction between RUN domain proteins including RUFY proteins (designated as RUN and FYVE domain-containing proteins) and several small GTPases with respect to the regulation of cell polarity and membrane trafficking on filamentous network.

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Figures

Figure 1
Figure 1
Cell polarity is observed in many cases. For example, neuronal cells are asymmetric with discrete regions responsible for different roles that may underlie the generation of specific compartments within cells, which is distinct in biochemical composition, function, and structure. An arrow indicates the direction of polarity.
Figure 2
Figure 2
Schematic illustration of intracellular vesicle transport. The model shows several pathways used by biosynthetic secretory and internalized endocytotic cargoes to reach their destinations. Note that some critical trafficking routes have been omitted for clarity.
Figure 3
Figure 3
Schematic diagram indicating the domain structures of the RUFY1, RUFY2, RUFY3, and RUFY4 proteins. The functionally important sites and their interaction proteins are shown. Genomic locations of each the genes and approximate molecular mass of each the proteins are also shown at the both ends. RUN = RPIP8, UNC-14, and NESCA proteins, FYVE = Fab-1, YGL023, Vps27, and EEA1 proteins, CC = Coiled Coil.
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