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PROSITE documentation PDOC51511 [for PROSITE entry PS51511]

FIP-RBD domain profile





Description

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.

Technical section

PROSITE method (with tools and information) covered by this documentation:

FIP_RBD, PS51511; FIP-RBD domain profile  (MATRIX)


References

1AuthorsJagoe W.N., Lindsay A.J., Read R.J., McCoy A.J., McCaffrey M.W., Khan A.R.
TitleCrystal structure of rab11 in complex with rab11 family interacting protein 2.
SourceStructure 14:1273-1283(2006).
PubMed ID16905101
DOI10.1016/j.str.2006.06.010

2AuthorsEathiraj S., Mishra A., Prekeris R., Lambright D.G.
TitleStructural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes.
SourceJ. Mol. Biol. 364:121-135(2006).
PubMed ID17007872
DOI10.1016/j.jmb.2006.08.064

3AuthorsShiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K., Wakatsuki S.
TitleStructural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1.
SourceProc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006).
PubMed ID17030804
DOI10.1073/pnas.0605357103

4AuthorsWei J., Liu Y., Bose K., Henry G.D., Baleja J.D.
TitleDisorder and structure in the Rab11 binding domain of Rab11 family interacting protein 2.
SourceBiochemistry 48:549-557(2009).
PubMed ID19119858
DOI10.1021/bi8020197



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