{PDOC51388}
{PS51388; GED}
{BEGIN}
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* GED domain profile *
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Dynamin superfamily  members  are  large  GTPases, conserved through evolution
mainly described  as  mechanochemical  enzymes  involved  in membrane scission
events. The  dynamin  superfamily  has  been subdivided into several subgroups
based on domain organization: classical dynamin, dynamin-like proteins (Dlps),
Mc proteins,  optic  atrophy  1  protein (OPA1), Mitofusins, guanylate-binding
proteins (GBP)  and  alastatins.  All members display a common architecture: a
large GTPase  (see  <PDOC00362>)  domain followed by a 'middle domain' of ill-
defined function  and  a  downstream  coiled-coil GTPase effector domain (GED)
that functions  in  higher  order  assembly and as a GTPase activating protein
(GAP) for  dynamin's  GTPase activity. Most members contain additional domains
that characterize  the  different  subgroups.  For example, classical dynamins
contain a  lipid  binding  Pleckstrin-homology  (PH)  (see <PDOC50003>) domain
between the  middle domain and the GED domain as well as a C-terminal proline-
arginine rich  domain (PRD) that interacts with numerous SH3 domain-containing
binding partners  while  Dlps  lack  the  PRD but have a PH domain, which may,
however, by  highly  divergent.  These  various  domains  confer  to dynamin a
variety of biochemical properties and cellular localizations, that may explain
the diversity  of  their biological implications in endocytosis, intracellular
traffic, organelle  fission  and  fusion,  cytokinesis and pathogen resistance
[1-4].

The GED  is  seen  to  be  largely  helical in nature, and its oligomerization
occurs via intermolecular packing of the helices [2].

The profile we developed covers the entire GED domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: June 2008 / First entry.

[ 1] Song B.D., Yarar D., Schmid S.L.
     "An assembly-incompetent mutant establishes a requirement for dynamin
     self-assembly in clathrin-mediated endocytosis in vivo."
     Mol. Biol. Cell. 15:2243-2252(2004).
     PubMed=15004222; DOI=10.1091/mbc.E04-01-0015
[ 2] Chugh J., Chatterjee A., Kumar A., Mishra R.K., Mittal R., Hosur R.V.
     "Structural characterization of the large soluble oligomers of the
     GTPase effector domain of dynamin."
     FEBS J. 273:388-397(2006).
     PubMed=16403025; DOI=10.1111/j.1742-4658.2005.05072.x
[ 3] Soulet F., Schmid S.L., Damke H.
     "Domain requirements for an endocytosis-independent, isoform-specific
     function of dynamin-2."
     Exp. Cell Res. 312:3539-3545(2006).
     PubMed=16938290; DOI=10.1016/j.yexcr.2006.07.018
[ 4] Charneau S., Bastos I.M.D., Mouray E., Ribeiro B.M., Santana J.M.,
     Grellier P., Florent I.
     "Characterization of PfDYN2, a dynamin-like protein of Plasmodium
     falciparum expressed in schizonts."
     Microbes Infect. 9:797-805(2007).
     PubMed=17533148; DOI=10.1016/j.micinf.2007.02.020

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