|PROSITE documentation PDOC50913 [for PROSITE entry PS50913]|
Golgins are Golgi-localized proteins that have an extended coiled-coil conformation, and play an important role in maintaining Golgi structure in all eukaryotic cells from yeast to humans. A subset of the golgins contain a carboxy-terminal region, called the GRIP domain, that mediates binding to Golgi membranes. The GRIP domain was named after the four proteins in which it is found and about which something has been reported (golgin-97, RanBP2-α, Imh1p and p230/golgin-245) [1,2].
ARL1 and ARL3 are required for localization of GRIP-domain proteins to Golgi membranes. ARL1-GTP interacts specifically with the GRIP domain to recruit it to membranes, and ARL3 is required for normal Golgi localization of ARL1 [3,4].
The profile we developed covers the whole GRIP domain.Last update:
July 2003 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Munro S. Nichols B.J.|
|Title||The GRIP domain - a novel Golgi-targeting domain found in several coiled-coil proteins.|
|Source||Curr. Biol. 9:377-380(1999).|
|Title||Membrane traffic: Arl GTPases get a GRIP on the Golgi.|
|Source||Curr. Biol. 13:R174-R176(2003).|
|3||Authors||Panic B. Whyte J.R. Munro S.|
|Title||The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts with vesicle-tethering factors at the Golgi apparatus.|
|Source||Curr. Biol. 13:405-410(2003).|
|4||Authors||Setty S.R. Shin M.E. Yoshino A. Marks M.S. Burd C.G.|
|Title||Golgi recruitment of GRIP domain proteins by Arf-like GTPase 1 is regulated by Arf-like GTPase 3.|
|Source||Curr. Biol. 13:401-404(2003).|