Dynamin and endocytosis.
The GTPase dynamin is essential for endocytosis, but its mechanism of action remains uncertain. Structures of its GTPase domain, as well as that of assembled dynamin, have led to major advances in understanding the structural basis of its mode of action. Novel data point more clearly than ever towards a role for this protein in the actin cytoskeleton, mitogen-activated protein kinase signaling and apoptosis, suggesting that dynamin might be a signaling GTPase.
Sever
Sanja
S
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School and Dana-Farber Cancer Institute, 1 Jimmy Fund Way, Boston, MA 02115, USA. sanja_sever@dfci.harvard.edu
D000818:Animals; D034281:Dynamins; D004705:Endocytosis; D020558:GTP Phosphohydrolases / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D015394:Molecular Structure; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D020558:GTP Phosphohydrolases; D034281:Dynamins