|PROSITE documentation PDOC51511 [for PROSITE entry PS51511]|
The Rab11 GTPase regulates recycling of internalized plasma membrane receptors and is essential for completion of cytokinesis. A family of Rab11 interacting proteins (FIPs) that conserve a C-terminal Rab-binding domain (RBD) selectively recognize the active form of Rab11. FIPs are diverse in sequence length and composition toward their N-termini, presumably a feature that underpins their specific roles in Rab11-mediated vesicle trafficking. They have been divided into three subfamilies (classe I, II, and III)on the basis of domain architecture. Class I FIPs comprises a subfamily of three proteins (Rip11/pp75/FIP5, Rab-coupling protein (RCP), and FIP2) that possess an N-terminal C2 domain (see <PDOC00380>), localize to recycling endosomes, and regulate plasma membrane recycling. The class II subfamily consists of two proteins (FIP3/eferin/arfophilin and FIP4) with tandem EF hands (see <PDOC00018>) and a proline-rich region. Class II FIPs localize to recycling endosomes, the trans-Golgi network, and have been implicated in the regulation of membrane trafficking during cytokinesis. The class III subfamily consists of a single protein, FIP1, which does not contain obvious homology domains or motifs other than the FIP-RBD [1,2,3,4].
The FIB-RBD domain consists of an N-terminal long α-helix, followed by a 90° bend at a conserved proline residue, a 3(10) helix and a C-terminal short β-strand, adopting an "L" shape (see <PDB:2D7C>). The long α-helix forms a parallel coiled-coil homodimer that symmetrically interacts with two Rab11 molecules on both sides, forming a quaternary Rab11-(FIP)2-Rab11 complex. The Rab11-interacting region of FIP-RBD is confined to the C-terminal 24 amino acids, which cover the C-terminal half of the long α-helix and the short β-strand [1,2,3,4].
The profile we developed covers the entire FIP-RBD domain.Last update:
November 2010 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Jagoe W.N., Lindsay A.J., Read R.J., McCoy A.J., McCaffrey M.W., Khan A.R.|
|Title||Crystal structure of rab11 in complex with rab11 family interacting protein 2.|
|2||Authors||Eathiraj S., Mishra A., Prekeris R., Lambright D.G.|
|Title||Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes.|
|Source||J. Mol. Biol. 364:121-135(2006).|
|3||Authors||Shiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K., Wakatsuki S.|
|Title||Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006).|
|4||Authors||Wei J., Liu Y., Bose K., Henry G.D., Baleja J.D.|
|Title||Disorder and structure in the Rab11 binding domain of Rab11 family interacting protein 2.|