• The amphiphysin SH3 domain when overexpressed in COS7 cells is a potent inhibitor of dynamin action when compared alongside other SH3 domains which binds to dynamin (Grb2, Spectrin and PLC g ) (see Wigge et al 1997 Current Biol. ). (endocytosis.org)
  • We isolated a new gene, ADL2, that encodes a dynamin-like protein in Arabidopsis. (deepdyve.com)
  • What makes amphiphysin a good candidate protein for dynamin recruitment? (endocytosis.org)
  • A mutation in a critical lipid binding residue of the PH domain ( Lys535Ala ) of dynamin leads to a dominant negative phenotype in cells (see Vallis et al 1999 ) but this can be partially rescued by a second mutation of the amphiphysin binding sequence in the PRD (see Vallis et al 1999 ) thus showing that the protein that interacts with this sequence plays an important role. (endocytosis.org)
  • It has been proposed that dynamin is a regulator (similar to classical G proteins) of downstream effectors. (ox.ac.uk)
  • Sequence analysis of ADL2 revealed a high degree of amino acid sequence similarity to other members of the dynamin superfamily. (deepdyve.com)
  • The first three superfamily members have been shown to oligomerise in vitro in the absence and presence of liposomes ( see electron microscopy comparison of dynamin family members ) and it is likely that the remaining members do likewise. (endocytosis.org)
  • Despite the low affinity of the amphiphysin-SH3 domain for dynamin ( Owen et al 1998 EMBO J. ) the interaction is likely to be considerably stronger in vivo where amphiphysin is a dimer and dynamin is an oligomer (see Wigge et al 1997 MBC ). (endocytosis.org)