Chaired by Richard Youle, NINDS

Balcony A, Natcher Conference Center

Important insights have been made recently into the molecular function and medical significance of the dynamin family of large GTPases. Dynamin mediates the membrane fission step of endocytotic vesicles budding from the plasma membrane. Around the tubular necks of endosomes dynamin forms spirals that change helical pitch upon binding GTP suggesting a mechanical process of membrane stretching and scission. Homologues of dynamin are involved in mitochondrial fission, apoptosis and viral resistance. One dynamin homologue localized predominantly to the ER and Golgi apparatus, atlastin-1, is mutated in one of the most common forms of the hereditary spastic paraplegias. The mini-symposium will cover the four prominent subclasses of the dynamin family with a focus on the molecular basis of defects in family members leading to neurologic diseases.

Program:

Structural Analysis of Dynamin Reveals a Mechanism for Membrane Constriction
Jenny Hinshaw, NIDDK

Regulation of the Outer Mitochondrial Membrane Dynamics by Dynamin-related Protein 1
Mariusz Karbowski, NINDS

Mx Proteins-distant Relatives of Dynamins: History and Perspectives
Heinz Arnheiter, NINDS

Pathogenesis of Hereditary Spastic Paraplegia Due to Mutations in the Atlastin GTPase
Craig Blackstone, NINDS