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PROSITE documentation PDOC51205 |
Rab proteins form a family of signal-transducing GTPases that cycle between active GTP-bound and inactive GDP-bound forms. The Rab5 GTPase is an essential regulator of endocytosis and endosome biogenesis. Rab5 is activated by GDP-GTP exchange factors (GEFs) that contain a VPS9 domain and generate the Rab5-GTP complex [1]. The VPS9 domain catalyzes nucleotide exchange on Rab5 or the yeast homolog VPS21. The domain has a length of ~140 residues and forms the central part of the yeast VPS9 (vacuolar protein sorting-associated) protein, which acts as a GEF for VPS21. Some domains which can occur in combination with the VPS9 domain are CUE (see <PDOC51140>), A20-type zinc finger (see <PDOC51036>), Ras-associating (RA) (see <PDOC50200>), SH2 (see <PDOC50001>), RCC1 (see <PDOC00544>), DH (see <PDOC00605>), PH (see <PDOC50003>), rasGAP (see <PDOC00438>), MORN and ankyrin repeat (see <PDOC50088>).
Structurally, the VPS9 domain adopts a layered fold of six α helices (see <PDB:1TXU>). Conserved residues from the fourth and sixth helices and the loops N-terminal to these helices form the surface that interacts with Rab5 and Rab21 [2].
Some proteins known to contain a VPS9 domain:
The profile we developed covers the entire VPS9 domain.
Last update:May 2006 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Carney D.S. Davies B.A. Horazdovsky B.F. |
Title | Vps9 domain-containing proteins: activators of Rab5 GTPases from yeast to neurons. | |
Source | Trends Cell Biol. 16:27-35(2006). | |
PubMed ID | 16330212 | |
DOI | 10.1016/j.tcb.2005.11.001 |
2 | Authors | Delprato A. Merithew E. Lambright D.G. |
Title | Structure, exchange determinants, and family-wide rab specificity of the tandem helical bundle and Vps9 domains of Rabex-5. | |
Source | Cell 118:607-617(2004). | |
PubMed ID | 15339665 | |
DOI | 10.1016/j.cell.2004.08.009 |